Recombinant Mouse Kallikrein-8 (KLK8) Protein (His)

Name: Recombinant Mouse Kallikrein-8 (KLK8) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03204P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Mouse Kallikrein-8 (KLK8) 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	Q61955
Target Symbol	KLK8
Synonyms	Klk8; Nrpn; Prss19Kallikrein-8; mK8; EC 3.4.21.118; Neuropsin; NP; Serine protease 19
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	ILEGRECIPHSQPWQAALFQGERLICGGVLVGDRWVLTAAHCKKQKYSVRLGDHSLQSRDQPEQEIQVAQSIQHPCYNNSNPEDHSHDIMLIRLQNSANLGDKVKPVQLANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCDGMLQGITSWGSDPCGKPEKPGVYTKICRYTTWIKKTMDNRD
Expression Range	33-260aa
Protein Length	Full Length of Mature Protein
Mol. Weight	27.1kDa
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

Target Function	Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury.
Subcellular Location	Secreted. Cytoplasm. Note=Shows a cytoplasmic distribution in the keratinocytes.
Protein Families	Peptidase S1 family, Kallikrein subfamily
Database References	KEGG: mmu:259277 STRING: 10090.ENSMUSP00000082588 UniGene: PMID: 22520925 Klk8 is involved in the proliferation and migration of keratinocytes through Klk6 in the early stages of wound healing, and possibly in keratinocyte differentiation associated with the upregulation of PAR2 in the late stages of wound healing. PMID: 22358061 KLK8 is involved in synaptic tagging during LTP at basal and apical dendritic inputs. PMID: 21646406 the serine protease neuropsin is critical for stress-related plasticity in the amygdala by regulating the dynamics of the EphB2-NMDA-receptor interaction, the expression of Fkbp5 and anxiety-like behaviour PMID: 21508957 Klk8 might thus be involved in tissue development and rearrangement. PMID: 20180635 role of loop structures in the activity of serine protease and regulated secretion PMID: 11854276 Neuropsin was localized extracellularly in neuronal cell bodies and their neurites in mouse hippocampus. Neuropsin may be involved in neurite outgrowth during the development of the nervous system. PMID: 11880192 gene expression of a serine-protease neuropsin in the mouse vagina, and as a marker of the estrogen-independent persistent proliferation and cornification of the vaginal epithelium PMID: 12354676 Neuropsin is the first extracellular protease to show the evident induction of expression and activity by decidualization and might contribute to the remodeling of extracellular components after decidualization. PMID: 12390870 mouse MCs store at least two distinct families of tryptic-like proteases in their secretory granules, including PRSS19 PMID: 12646205 Presynaptic adhesion molecule L1 is a substrate for neuropsin in the hippocampus. PMID: 12944500 study demonstrates changes in the expression of neuropsin and protease M/neurosin in oligodendrocytes following hemisection of the spinal cord PMID: 15378660 Neuropsin-/- mice showed attenuated demyelination and delayed oligodendroglial death early during the course of autoimmune encephalomyelitis PMID: 15920728 Nrpn is necessary for establishment of LTP and has a significant role in memory acquisition. PMID: 16308352 These observations suggest that neuropsin is involved in the secondary phase of the pathogenesis of SCI mediated by demyelination, oligodendrocyte death, and axonal degeneration. PMID: 17629414 Neuropsin-dependent late associativity is particularly important in nonstressful associative memory. PMID: 18216192 Increased anxiety-like behavior in neuropsin (kallikrein-related peptidase 8) gene-deficient mice. PMID: 18513120

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.