Recombinant Human METAP1D Protein (His Tag)

Name: Recombinant Human METAP1D Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3348
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NP_954697.1
Synonym	MAP 1D, MAP1D, MetAP 1D, Metap1l
Background	Methionine aminopeptidase 1D, also known as MAP1D, is a member of thepeptidase M24A family. N-terminal methionine removal is an important cellular process required for proper biological activity, subcellular localization, and eventual degradation of many proteins. The enzymes that catalyze this reaction are called Methionine aminopeptidases (MAPs). MAP1D is overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level). Downregulation of MAP1D expression by shRNA in HCT-116 colon carcinoma cells reduces anchorage-independant growth in soft agar. MAP1D binds two cobalt ions per subunit. The true nature of the physiological cofactor is under debate. MAP1D is also active with zinc, manganese or divalent ions. MAP1D removes the amino-terminal methionine from nascent proteins. It may also play an important role in colon tumorigenesis.
Description	A DNA sequence encoding the human MAP1D (NP_954697.1) (Arg 44-Ala 335) was expressed, with an initial Met at the N-terminus and a His tag at the C-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Arg 44-Ala 335
Molecular Weight	The secreted recombinant human MAP1D consists of 303 a.a. and predicts a molecular mass of 33.4 kDa. It migrates as an approximately 36 kDa band in SDS-PAGE under reducing conditions.
Purity	>92% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measure by its ability to remove methionine from a fluorogenic peptide substrate H-Met-Gly-Pro-AMC, R&D Systems, Catalog#ES017. The resulting GP-AMC is cleaved by human DPPIV/CD26, R&D Systems, Catalog#1180SE. The specific activity is >30 pmoles/min/ug.
Formulation	Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.