Recombinant Human B-Cell Receptor-Associated Protein 31 (BCAP31) Protein (GST)

Name: Recombinant Human B-Cell Receptor-Associated Protein 31 (BCAP31) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02351P
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	Recombinant Human B-Cell Receptor-Associated Protein 31 (BCAP31) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P51572
Target Symbol	BCAP31
Synonyms	6C6 AG; 6C6 AG tumor associated antigen; 6C6-AG tumor-associated antigen; 6C6AG; 6C6AG tumor associated antigen; Accessory protein BAP 31; Accessory protein BAP31; B cell receptor associated protein 31; B-cell receptor-associated protein 31; BA31; BAP 31; Bap31; BAP31_HUMAN; BCAP 31; BCAP31; BCR associated protein Bap 31; BCR associated protein Bap31; BCR-associated protein 31; CDM; CDM protein; DXS1357E; MS950; p28; p28 Bap31; Protein CDM; RP23-329M9.5
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	SLQWTAVATFLYAEVFVVLLLCIPFISPKRWQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTEKVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVKLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVDGPMDK
Expression Range	2-243aa
Protein Length	Partial
Mol. Weight	54.5kDa
Research Area	Apoptosis
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	Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by stimulating the translocation of NDUFS4 and NDUFB11 from the cytosol to the mitochondria via interaction with TOMM40. In response to ER stress, delocalizes from the ER-mitochondria contact sites and binds BCL2. May be involved in CASP8-mediated apoptosis.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein.
Protein Families	BCAP29/BCAP31 family
Database References	HGNC: 16695 OMIM: 300398 KEGG: hsa:10134 STRING: 9606.ENSP00000392330 UniGene: PMID: 29653744 BAP31 expression is an independent prognostic factor for overall survival of patients with postoperative hepatocellular carcinoma (HCC), and low expression levels of BAP31 in HCC may indicate poor outcomes of HCC patient after surgical resection. PMID: 25980696 results suggest that enhanced expression of csBAP31 contributes to poor survival of NSCLC cells PMID: 29145450 This patient's clinical features, muscle histopathology, brain MRI features, and family history were suggestive of mitochondrial encephalopathy. Whole exome sequencing research study confirmed the diagnosis of BCAP31-associated encephalopathy, DDCH syndrome. PMID: 28332767 Data characterized the biochemical properties of plant orthologs of human B-cell receptor-associated protein BAP31 (HsBAP31) termed 'plant BAP-like proteins' (PBL proteins). PMID: 27770627 Data show that tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced endoplasmic reticulum (ER) stress was triggered by caspase-8-mediated cleavage of B cell receptor-associated protein 31 (BAP31). PMID: 26212606 The C-terminal domain of BAP31 is exposed on the cell surface of human embryonic stem cells. PMID: 26102500 both BCAP31 and ABCD1 were associated with hepatic cholestasis and death before 1 year. Remarkably, a patient with an isolated deletion at the 3'-end of SLC6A8 had a similar severe phenotype as seen in BCAP31 deficiency PMID: 24597975 Transfected human respiratory syncytial virus SH protein co-localizes with transfected BAP31 in cells, and pulls down endogenous BAP31. PMID: 25854864 In the titel. PMID: 25044748 These findings provide, for the first time, mechanistic insights into how BAP31 regulates human embryonic stem cell stemness and survival via control of EpCAM expression. PMID: 24898727 Hypomethylation in BCAP31 is associated with breast cancer. PMID: 24395279 the lack of BAP31 disturbs endoplasmic reticulum (ER) metabolism and impacts the Golgi apparatus, highlighting an important role for BAP31 in ER-to-Golgi crosstalk. PMID: 24011989 BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol. PMID: 21947079 Membrane-Associated RING-CH proteins MARCH VIII and MARCH IV associate with Bap31 and target CD81 and CD44 to lysosomes PMID: 21151997 Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction. PMID: 21183955 Contiguous deletion of the X-linked adrenoleukodystrophy gene (ABCD1) and DXS1357E: a novel neonatal phenotype similar to peroxisomal biogenesis disorders. PMID: 11992258 CASP8 cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. PMID: 12668660 Data describe a novel human member of the protein tyrosine phosphatase-like B (PTPLB) family, an integral protein of the endoplasmic reticulum membrane, as a BAP31-interacting protein. PMID: 15024066 Cleavage of BAP31 leads to the generation of ER- localized, proapoptotic BAP20, which may mediate mitochondrion-ER cross talk through a Ca(2+)-dependent mechanism PMID: 15254227 BAP31 may play a role in regulating intracellular trafficking of CD11b/CD18 in neutrophils PMID: 15294914 We have characterized a molecular mechanism by which calnexin regulates ER-stress-mediated apoptosis in a manner independent of its chaperone functions but dependent of its binding to Bap31. PMID: 16858427 Bap31 performs quality control on class I molecules in two distinct phases: by exporting peptide-loaded class I molecules to the ER/Golgi, and by retrieving class I molecules that have lost peptides in the acidic post-ER environment. PMID: 17056546 Bap31 is a component of the endoplasmic reticulum (ER) quality control compartment and that it moves between the peripheral ER and a juxtanuclear ER or ER-related compartment distinct from the conventional ER-Golgi intermediate compartment. PMID: 18287538 BAP31 associates with the N terminus of one of its newly synthesized client proteins, the DeltaF508 mutant of CFTR, and promotes its retrotranslocation from the endoplasmic reticulum and degradation by the cytoplasmic 26S proteasome system. PMID: 18555783 Results identify B-cell-associated protein 31 as a novel binding partner of the high-risk human papillomavirus 16 E5 proteins and provide insight into how the E5 proteins may modulate the life cycle in differentiating cells. PMID: 18684816

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.