Recombinant Dog Caveolin-1 (CAV1) Protein (His)

Name: Recombinant Dog Caveolin-1 (CAV1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10846P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Dog Caveolin-1 (CAV1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P33724
Target Symbol	CAV1
Synonyms	CAV1; CAVCaveolin-1; Vesicular integral-membrane protein VIP21
Species	Canis lupus familiaris (Dog) (Canis familiaris)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMAEEMSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPFFEAVGKIFSNIRINMQKET
Expression Range	1-178a
Protein Length	Full Length
Mol. Weight	22.6kDa
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	May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation.
Subcellular Location	Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Membrane raft. Golgi apparatus, trans-Golgi network.
Protein Families	Caveolin family
Database References	KEGG: cfa:403980 STRING: 9615.ENSCAFP00000005060 UniGene: Cfa.3850

Gene Functions References

results demonstrate that knockdown of EPLIN or Cav-1 substantially suppresses apical extrusion of transformed cells, implying that the expression of these molecules is required for the elimination of newly emerging transformed cells from the epithelium. PMID: 25609711
Early intervertebral disc degeneration involves down-regulation of Caveolin-1 expression PMID: 23360510
To better understand the role of caveolin-1 in bone homeostasis and response to beta-TCP scaffold, beta-TCP was implanted into mandible defects, and gene expression profiles were examined focused on the molecular components involved in caveolin-1 regulation. PMID: 23401359
Malignant mammary cells showed a loss of Cav-1 expression. Our findings indicate that Cav-1 is a potential prognostic marker for canine mammary tumors. PMID: 22370882
Alcohol promotes the myocardial oxidative stress and fibrosis through an elevated expression of PYK2 and a lowered expression of caveolin-1. PMID: 21914371
Diminished function of human BCRP transfected into MDCK cells after canine Cav1 knockdown is likely mediated by alterations in protein-protein interactions and suggests a positive regulation of BCRP function by CAV1. PMID: 20936466
these is a strong correlation between Cav-1-positive breast carcinomas and shorter overall survival in dogs. PMID: 20153868
RNAi-mediated Cav-1 knock-down results in a decrease in virus titre in infected Madin-Darby canine kidney cells. PMID: 20504340
These findings link increased expression of Cav-1 to neoplastic transformation and suggest that Cav-1 expression is associated with more malignant canine mammary tumours and their vascular invasion and regional lymph node metastasis. PMID: 20153867
caveolin-1 does not play a major role in lipid raft-mediated biosynthetic membrane trafficking PMID: 16260622
EGF-based signaling cascades phosphorylate Cav1 and have roles in caveolae assembly PMID: 16332692
These data suggest that, upon stimulation, Galpha(q)(GTP) switches from having strong interactions with Gbetagamma to Cav1, thereby releasing Gbetagamma. PMID: 18397999

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.