Recombinant Human Protein Transport Protein Sec16A (SEC16A) Protein (His)

Name: Recombinant Human Protein Transport Protein Sec16A (SEC16A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09944P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Protein Transport Protein Sec16A (SEC16A) 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	O15027
Target Symbol	SEC16A
Synonyms	SEC16A; KIAA0310; SEC16; SEC16L; Protein transport protein Sec16A; SEC16 homolog A; p250
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSMPKTVQAAPPALPGPPGAPVNMYSRRAAGTRARYVDVLNPSGTQRSEPALAPADFVAPLAPLPIPSNLFVPTPDAEEPQLPDGTGREGPAAARGLANPEPAPEPKVLSSAASLPGSELPSSRPEGSQGGELSRCSSMSSLSREVSQHFNQAPGDLPAAGGPPSGAMPFYNPAQ
Expression Range	1943-2154aa
Protein Length	Partial
Mol. Weight	26.1kDa
Research Area	Transport
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	Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. Mediates the recruitment of MIA3/TANGO to ERES. Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane. Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183. Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the cell membrane in adipocytes.
Subcellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cytoplasm, perinuclear region. Cytoplasm, cytosol. Microsome membrane.
Protein Families	SEC16 family
Database References	HGNC: 29006 OMIM: 612854 KEGG: hsa:9919 STRING: 9606.ENSP00000325827 UniGene: Hs.522500
Tissue Specificity	Ubiquitous. Expressed at higher levels in the pancreas.

Gene Functions References

these findings highlight a novel function of Sec16A as an essential mediator of endoplasmic reticulum stress-associated unconventional secretion. PMID: 28067262
Sec16A also stabilized the interacting ubiquitin ligase RNF152, which localizes to the lysosome and has structural similarity with RNF183 PMID: 29300766
Mammalian endoplasmic reticulum exit sites are organized by TANGO1 acting as a scaffold, in cooperation with Sec16 for efficient secretion. PMID: 28442536
Results suggest that it is the presence of rare syntenic SEC16A and MAMDC4 deletions that increases susceptibility to axial spondyloarthritis in family members who carry the HLA-B*27 allele. PMID: 25956157
growth factors modulate Sec16 protein levels and dynamics. Sec16 acts as part of a coherent feed-forward loop, which integrates secretion and growth factor signaling. PMID: 25526736
LRRK2 regulates the anterograde endoplasmic reticulum (ER)-Golgi transport through anchoring Sec16A at the endoplasmic reticulum exit sites (ERES). PMID: 25201882
Sec16A remains associated with endoplasmic reticulum exit sites throughout mitosis. PMID: 21045114
Sar1-GTP-dependent assembly of Sec16 on the endoplasmic reticulum(ER) membrane forms an organized scaffold defining ER exit sites PMID: 17005010
Mammalian cells contain two distinct Sec16 homologues: a large protein Sec16L of 2154 aa and a smaller protein Sec16S of 1060 aa. PMID: 17192411
Results suggest that KIAA0310p, a mammalian homologue of yeast Sec16, builds up endoplasmic reticulum (ER) exit sites in cooperation with p125 and plays a role in membrane traffic from the ER. PMID: 17428803
These data are consistent with a model where Sec16 acts as a platform for COPII assembly at endoplasmic reticulum exit sites. PMID: 19638414

FAQs

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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.

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