Recombinnant Human Protein Lin-28 Homolog A (LIN28A) Protein (His)

Name: Recombinnant Human Protein Lin-28 Homolog A (LIN28A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07069P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinnant Human Protein Lin-28 Homolog A (LIN28A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9H9Z2
Target Symbol	LIN28A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	HGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGP
Expression Range	39-112aa
Protein Length	Partial
Mol. Weight	9.5 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism. Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 AND tut7 uridylyltransferaseS. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells. Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue.
Subcellular Location	Cytoplasm. Rough endoplasmic reticulum. Cytoplasm, P-body. Cytoplasm, Stress granule. Nucleus, nucleolus.
Protein Families	Lin-28 family
Database References	HGNC: 15986 OMIM: 611043 KEGG: hsa:79727 STRING: 9606.ENSP00000254231 UniGene: PMID: 30196987 Data indicated that LIN28A might make contribution to HSF proliferation and extracellular matrix synthesis upon thermal injury. PMID: 28771809 LIN28A inhibits lysosomeassociated membrane glycoprotein 1 protein expression in embryonic stem and bladder cancer cells. PMID: 29749495 Studied effects of lin-28 homolog A protein (Lin28A) on cells proliferation, migration, invasion and apoptosis of osteocarcinoma (OS) cells through metastasis associated lung adenocarcinoma transcript 1 (MALAT1). PMID: 29204769 Pig induced pluripotent stem cell (piPSC) line was generated from embryonic fibroblast cells using retroviral transduction approaches carrying human transcriptional factors: OCT4, SOX2, KLF4, c-MYC and LIN28. PMID: 29034889 LIN28A is a sensitive IHC marker for the diagnosis of Embryonal Tumor with Multilayered Rosettes , but immunoreactivity can also be seen in a proportion of Atypical Teratoid/Rhabdoid Tumors PMID: 28744687 Recent improvement in high-throughput sequencing has highlighted the potential role of LIN28/let-7 regulatory network in several developmental events. It was proposed that this pathway might represent a functional signature in cell proliferation, transition between commitment and pluripotency, and regulation of cancer and tumorigenicity. PMID: 28846452 Knockdown of miR-128a induces Lin28a expression and reverts myeloid differentiation blockage in acute myeloid leukemia. PMID: 28569789 Lin28A and Lin28B are co-expressed colon cancer tissues and have functional similarities. PMID: 27793004 this study demonstrates that Lin28A can activates androgen receptor via regulation of c-myc and promotes malignancy of ER-/Her2+ breast cancer PMID: 27494865 The results suggest that the Lin28a gene enhances the osteoblastic differentiation of human periosteum-derived cells. In addition, the Lin28a gene increases mitochondrial activity in human periosteum-derived cells. PMID: 29143345 High LIN28A expression is associated with pancreatic cancer. PMID: 26910839 the specific interaction between zinc knuckle domain of LIN28 and pre-let-7 is necessary and sufficient to induce oligouridylation. PMID: 28297670 It has been shown that the constitutive expression of Lin28a during neuronal differentiation in vitro positively and negatively affects numerous miRNAs. PMID: 27881476 ur study demonstrated that disturbance of the let-7/LIN28 double-negative feedback loop is involved in the regulation of radio- and chemo-resistance, and that let-7 and LIN28 could be employed as predictive biomarkers of response to radiotherapy or chemotherapy in non-small-cell lung cancer patients. PMID: 28235063 tight control by ESE3/EHF over the Lin28/let-7 axis is a critical barrier to malignant transformation. PMID: 27197175 MSI2 might play a crucial role in sustaining stemness and chemoresistance of liver cancer stem cells in LIN28A-dependent manner in hepatocellular carcinoma. PMID: 27721018 High LIN28A expression is associated with colorectal cancer. PMID: 27859935 LIN28A and LIN28B play cooperative roles in regulating reprogramming, naive/primed pluripotency, and stem cell metabolism. PMID: 27320042 The molecular dynamics simulations suggest that a conserved structural feature of the loop regions of pre-let-7 miRNAs is more important for LIN28 recognition than sequence conservation among members of the let-7 family or the presence of the GGAG motif in the 3' region. PMID: 28076679 Lin28A is up-regulated in 73.3 % of colon cancer patients. Lin28A-enforced expression in colon cancer cells enhanced the chemosensitivity of cancer cells to 5-FU via promoting apoptosis in a let-7 independent manner, associated with decreasing the expression of DNA damage repair protein H2AX. PMID: 26687759 Upregulation of let-7a carries the potential to reverse CCL18 induced cell proliferation and migration alteration in breast cancer cells by regulating Lin28 expression. PMID: 26898455 Data suggest that the Lin28/let-7 (lin-28 homolog protein/mirnlet7 microRNA) molecular switch plays roles in regulation of cell growth signaling pathways and in regulation of expression of metabolic enzymes. [REVIEW] PMID: 26811207 Lin28A expression promotes metabolic switching to a phenotype that relies predominantly on glycolysis as an energy source, while compromising oxidative phosphorylation. PMID: 27230676 high LIN28 expressing ovarian cancer cells secrete exosomes that can be taken up by nontumor cells and cause changes in gene expression and cell behavior associated with tumor development. IGROV1 PMID: 26583126 data document the expression profiles of the Lin28/let-7 system in rat testis along postnatal/pubertal maturation, and their perturbation in models of pubertal and hormonal manipulation PMID: 26494358 The role of Lin28 in cancer and immunity. [Review] PMID: 26945970 Erythroid-Specific Expression of LIN28A Is Sufficient for Robust Gamma-Globin Gene and Protein Expression in Adult Erythroblasts. PMID: 26675483 Our findings suggest that Lin28 plays a key role in the acquisition of resistance to AR-targeted therapies by prostate cancer cells and establish the importance of Lin28 in prostate cancer progression. PMID: 26714839 LIN28 may regulate splicing and gene expression programs that drive breast cancer subtype phenotypes. PMID: 26149387 Data implicate LIN28/RAS/MAP kinase as key drivers of tumorigenesis atypical teratoid rhabdoid tumors. PMID: 25638158 LIN28 and its regulatory microRNAs have roles in adult adrenocortical cancer PMID: 25200669 LIN28A over-expression increased HbF, reduced beta (sickle)-globin, and strongly suppressed all members of the let-7 family of miRNAs while reducing erythrocyte sickling. PMID: 25188417 Lin28A and Lin28B enhance, whereas let-7 suppresses, aerobic glycolysis via targeting pyruvate dehydrogenase kinase 1, or PDK1. PMID: 25301052 Expression of SUMO1/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28/let-7. PMID: 24942926 Results show the expression of Lin28 closely associated with resistance to paclitaxel in Hep3B cells which expresses high levels of Lin28. Its dysregulation inhibited let-7 family microRNA levels and upregulated the Bcl-xL, which is a target of let-7. PMID: 24970027 Incubation of a embryonal carcinoma cell line with N-methyl-mesoporphyrin IX reduces its stem cell traits. In particular it decreases OCT4, HMGA1, CCNB1, CDK4, and Lin28A protein, decreases sphere formation, and inhibits colony formation. PMID: 26045559 DFMO treatment restores balance to the LIN28/Let-7 axis and inhibits glycolytic metabolism and neurosphere formation in neuroblastoma PMID: 25415050 overexpression of Lin28 can suppress the biological behavior of gastric cancer in vitro, and let-7 miRNA may play an important role in the process PMID: 25515921 methylation modulates pluripotency in embryonic stem cells PMID: 25479749 Trim25 binds to the conserved terminal loop (CTL) of pre-let-7 and activates TuT4, allowing for more efficient Lin28a-mediated uridylation. PMID: 25457611 Intraocular medulloepitheliomas and embryonal tumors with multilayered rosettes of the brain both display LIN28A positivity. Only the latter, however, display amplification of the 19q13.42 locus involving C19MC PMID: 25748578 detected aberrant expression of LIN28A and/or LIN28B in 38% of a large series of human CRC samples (n = 595), where LIN28 expression levels were associated with invasive tumor growth PMID: 25956904 High Lin28 expression is associated with gastric cancer. PMID: 25128063 Lin28 induced EMT in breast cancer cells via downregulation of let-7a. PMID: 24349438 High LIN28 expression was an independent prognostic factor for a shorter survival in glioblastoma multiforme patients. PMID: 24475120 Results highlight a novel molecular interaction between miR-125b and Lin28 in glioblastoma stem cells. PMID: 24356103 The results have demonstrated that LIN28 is a key translational determinant of the initiation of human embryonic stem cell differentiation. PMID: 24860167 High LIN28 expression is associated with embryonal tumor with multilayered rosettes. PMID: 24311633 Data suggest that LIN28A plays functional role in regulating trophoblast differentiation/placentation; loss of LIN28A in human trophoblasts is sufficient to induce differentiation, but loss of Lin28a does not induce mouse trophoblast differentiation. PMID: 24006280

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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