Recombinant Human Chymotrypsin-Like Elastase Family Member 2B (CELA2B) Protein (His)

Name: Recombinant Human Chymotrypsin-Like Elastase Family Member 2B (CELA2B) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10993P
Price: 349.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Price Save $1,055

Size

100ug

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Product Overview

Description	Recombinant Human Chymotrypsin-Like Elastase Family Member 2B (CELA2B) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P08218
Target Symbol	CELA2B
Synonyms	CELA2B; ELA2B; Chymotrypsin-like elastase family member 2B; EC 3.4.21.71; Elastase-2B
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His
Target Protein Sequence	MLGGEEARPNSWPWQVSLQYSSNGQWYHTCGGSLIANSWVLTAAHCISSSGIYRVMLGQHNLYVAESGSLAVSVSKIVVHKDWNSDQVSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGALPDDLKQGQLLVVDYATCSSSGWWGSTVKTNMICAGGDGVICTCNGDSGGPLNCQASDGRWEVHGIGSLTSVLGCNYYYKPSIFTRVSNYNDWINSVIANN
Expression Range	29-269aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.4
Research Area	Cell Biology
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.
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 upon elastin.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family, Elastase subfamily
Database References	HGNC: 29995 OMIM: 609444 KEGG: hsa:51032 STRING: 9606.ENSP00000365075 UniGene: Hs.631871
Tissue Specificity	Pancreas.

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.