Recombinant Human Semenogelin-1 (SEMG1) Protein (His-SUMO)

Name: Recombinant Human Semenogelin-1 (SEMG1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02801P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Semenogelin-1 (SEMG1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P04279
Target Symbol	SEMG1
Synonyms	Alpha-Inhibin-31; Alpha-Inhibin-92; Cancer/testis antigen 103; CT103; dJ172H20.2 (semenogelin I); dJ172H20.2; MGC14719; Semen coagulating protein; Semenogelin; Semenogelin I; SEMG; SEMG1; SEMG1_HUMAN; Seminal basic protein; seminal vesicle secretory protein 5; SgI; Svp-1; Svp5; SVPIIA; Svs2; SVS2P; Svs2p2; Svs5
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	QKGGSKGRLPSEFSQFPHGQKGQHYSGQKGKQQTESKGSFSIQYTYHVDANDHDQSRKSQQYDLNALHKTTKSQRHLGGSQQLLHNKQEGRDHDKSKGHFHRVVIHHKGGKAHRGTQNPSQDQGNSPSGKGISSQYSNTEERLWVHGLSKEQTSVSGAQKGRKQGGSQSSYVLQTEELVANKQQRETKNSHQNKGHYQNVVEVREEHSSKVQTSLCPAHQDKLQHGSKDIFSTQDELLVYNKNQHQTKNLNQDQQHGRKANKISYQSSSTEERRLHYGENGVQKDVSQRSIYSQTEKLVAGKSQIQAPNPKQEPWHGENAKGESGQSTNREQDLLSHEQKGRHQHGSHGGLDIVIIEQEDDSDRHLAQHLNNDRNPLFT
Expression Range	24-402aa
Protein Length	Full Length of Mature Protein
Mol. Weight	58.8kDa
Research Area	Cell Biology
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	Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA.; Alpha-inhibin-92 and alpha-inhibin-31, derived from the proteolytic degradation of semenogelin, inhibit the secretion of pituitary follicle-stimulating hormone.
Subcellular Location	Secreted.
Protein Families	Semenogelin family
Database References	HGNC: 10742 OMIM: 182140 KEGG: hsa:6406 STRING: 9606.ENSP00000361867 UniGene: PMID: 25027395 Peptides from the antimicrobial protein semenogelin I have antibacterial activity. PMID: 18314226 EPPIN and SEMG1 rapidly co-evolved in primates PMID: 24312623 SEMG1 was significantly changed in asthenozoosperm, which could be the candidate gene for the development of diagnostic marker and provided the opportunity to further illustrate the biological mechanisms of asthenozoospermia. PMID: 23289976 Three regions of SEM1(86-107) comprise the amyloid fibril core that enhances HIV-1 infection. PMID: 24811874 Interaction analysis identifies semenogelin I fragments as new binding partners of PIP in human seminal plasma PMID: 23085372 EPPIN's semenogelin I binding site: a contraceptive drug target. PMID: 22699487 Nuclear semenogelin I expression could be a reliable prognosticator in men who undergo radical prostatectomy. PMID: 22617231 The proteomes of the type-1 diabetic, type-2 diabetic, and non-diabetic obese patients presented elevated amounts of the same set of one molecular form of semenogelin-1, one form of clusterin, and two forms of lactotransferrin. PMID: 21525168 Peptides released by physiological cleavage of Semg1 and Semg2 form amyloids that enhance HIV infection. PMID: 22177559 These results suggest the involvement of semenogelins in prostate cancer and their prognostic values in predicting cancer progression after radical prostatectomy. PMID: 21557275 Spermatozoa interact with semenogelin I in solution in a non-Zn2+-dependent manner, but associate with immobilized semenogelin I only in the presence of Zn2+. PMID: 20378931 Cysteine 239 of rSEMG1 appears to be the critical amino acid for both binding to eppin and inhibiting sperm motility. PMID: 19889947 Transcripts in the gastro-intestinal tract and skeletal muscle almost exclusively encoded SgI PMID: 12200457 Seminal plasma motility inhibitor, one of the fragments of Sg, has its inhibitory effect on ejaculated spermatozoa in liquefied semen under physiological conditions. PMID: 14581514 peptides produced by cleavage of semenogelin I, the predominant human semen coagulum protein, had high levels of antibacterial activity. PMID: 14613901 structural changes in the semenogelin 1 and 2 proteins that have arisen since the human-chimpanzee-gorilla split may be responsible for the physiological differences between these species ejaculated semen that correlate with their sociosexual behavior PMID: 14629036 The binding of Zn2+ to SgI and SgII and their involvment in regulating the activity of PSA are reported. PMID: 15563730 in seminal plasma and on spermatozoa following ejaculation, Eppin is bound to semenogelin I PMID: 15590901 Authors analyzed an intronic T9 repeat of semenogelin I (SEMG1) and report mutation frequencies of 51% (75 of 146) and 62% (8 of 13) in MMR-deficient primary colorectal cancers and cell lines, respectively. PMID: 15930278 The study provides evidence that senile seminal vesicle amyloid is derived from SgI; this form of amyloidosis was provisionally designated as ASgI. PMID: 15962837 truncated (lacking 60 amino acids ) & wild-type semenogelin molecules had similar Zn(2+)-binding properties & they showed also similar susceptibility for degradation by prostate-specific antigen PMID: 16582407 The semenogelin-CD52 soluble form is a direct consequence of the liquefaction process in human semen. PMID: 17624925 The conformational change induced in semenogelin I by the binding of Zn(2+) may contribute to the ability of this protein to form a gel PMID: 17680810 SGI is a novel target for protein S-nitrosylation in spermatozoa. PMID: 17683036 SEMG I expression in myeloma cells can be upregulated by 5-azacytidine, IL-4 and IL-6. PMID: 18468680 semenogelins I and II were directly cleaved by KLK14. Semenogelins were also able to reverse KLK14 inhibition by Zn2+, providing a novel regulatory mechanism for KLK14 activity. PMID: 18482984 antibacterial activity of the semenogelin-derived peptides generated in seminal plasma was strictly zinc-dependent both at neutral and low pH PMID: 18714013 Semenogelins (Sgs) modifies the membrane structure, indirectly inhibiting motility, and provides suggestions for a therapy for male infertility through selection of a functional sperm population using Sgs. PMID: 19089943 expressed in 46% of patients with early stage chronic lymphocytic leukemia; potential target for cancer vaccines PMID: 19241194

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.