Recombinant Human Carboxypeptidase D (CPD) Protein (hFc-Myc)

Name: Recombinant Human Carboxypeptidase D (CPD) Protein (hFc-Myc)
Brand: Beta LifeScience
SKU: BLC-01314P
Price: 299.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Price Save $1,456

Size

100ug

Product Overview

Description	Recombinant Human Carboxypeptidase D (CPD) Protein (hFc-Myc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O75976
Target Symbol	CPD
Synonyms	Metallocarboxypeptidase D gp180
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFC-Myc
Target Protein Sequence	GVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFYRLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRP
Expression Range	383-461aa
Protein Length	Partial
Mol. Weight	37.3 kDa
Research Area	Signal Transduction
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

Subcellular Location	Cell membrane; Single-pass type I membrane protein.
Protein Families	Peptidase M14 family
Database References	HGNC: 2301 OMIM: 603102 KEGG: hsa:1362 STRING: 9606.ENSP00000225719 UniGene: Hs.446079
Tissue Specificity	Highly expressed in placenta, pancreas and hepatoma cells. Lower levels found in skeletal muscle, heart and colon carcinoma and melanoma cell lines.

Gene Functions References

prolactin induction of VEGF-C and Runx2 was inhibited partly by Carboxypeptidase-D inhibitors, implicating nitric oxide , produced by PRL-regulated Carboxypeptidase-D, in breast cancer progression PMID: 28364216
Carboxypeptidase-D (CPD) overexpression coincides with high-grade lung cancer and the CPD overexpression could reverse the inhibitory effects of miR-214 PMID: 27494742
The human carboxypeptidase D transthyretin-like domain forms amyloid under physiological conditions. PMID: 25294878
Prolactin and R1881, acting through Stat5 and androgen receptor, act cooperatively to stimulate CPD gene transcription in breast cancer cells. PMID: 24433040
CPD immunostaining and testosterone/prolactin-stimulated CPD expression were higher in prostate cancer than benign tissues/cells. Elevated CPD increased NO production, which was abolished when both androgen and prolactin receptors were inhibited. PMID: 24615730
Carboxypeptidase D (CPD) is frequently upregulated in hepatocellular carcinoma; targeting CPD inhibits hepatocellular carcinoma cell proliferation through induction of G1 cell-cycle arrest and apoptosis. PMID: 23589395
Either high glucose or insulin (with low glucose) up-regulates beta-cell CPD (but not CPE). PMID: 21628999
Palmitoylation of carboxypeptidase D has a role in intracellular trafficking PMID: 12643288
The isolation and characterization of CPD from several haematopoietic tumour cells are reported. PMID: 15918796
First report to demonstrate carboxypeptidase D as part of the transforming growth factor (TGF)-beta pathway as a TGF-beta target gene implicated in the pathogenesis of lupus erythematosus. PMID: 17641957
prolactin or E2 up-regulated CPD mRNA and protein expression in MCF-7 breast cancer cells promoting their survival PMID: 18535109
CPD releases C-terminal Arg from peptides to provide the precursor substrate for inducible nitric oxide synthase, which enhances nitric oxide synthesis in macrophages. PMID: 11306718

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.