Analytical Data
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Gene name
COL12
- Application
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Alternative Names
COL12；CLP1；NSR2；SCARA4；Collectin-12
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9LJ44
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Expression Region
1-364aa
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AA Sequence
MEPKCDHCAT SQALIYCKSD LAKLCLNCDV HVHSANPLSH RHIRSLICEK CFSQPAAIRC LDEKVSYCQG CHWHESNCSE LGHRVQSLNP FSGCPSPTDF NRMWSSILEP PVSGLLSPFV GSFPLNDLNN TMFDTAYSMV PHNISYTQNF SDNLSFFSTE SKGYPDMVLK LEEGEEDLCE GLNLDDAPLN FDVGDDIIGC SSEVHIEPDH TVPNCLLIDK TNTSSFTGSN FTVDKALEAS PPGQQMNINT GLQLPLSPVL FGQIHPSLNI TGENNAADYQ DCGMSPGFIM SEAPWETNFE VSCPQARNEA KLRYKEKKLK RSFGKQIRYA SRKARADTRK RVKGRFVKAG DSYDYDPSSP TTNN
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
COL12 (Collagen Type XII) is a member of the collagen family, primarily identified in connective tissues, particularly in the extracellular matrix (ECM) of various tissues such as skin, tendons, and cartilage. Its unique structure features a triple helical domain, which is crucial for collagen stability and functionality. Research into COL12 has gained momentum due to its significant role in tissue organization, tensile strength, and cell adhesion. Notably, COL12 is implicated in various pathophysiological conditions, including fibrosis and certain types of cancer, where abnormal collagen deposition can influence tumor behavior and progression. Studies have shown that COL12 may also interact with other collagens and ECM components, highlighting its importance in maintaining the structural integrity of tissues. Moreover, its involvement in diverse biological processes prompts investigations into its potential as a biomarker for disease diagnosis or prognosis. Current research has focused on characterizing recombinant COL12 proteins to explore their functional roles and therapeutic applications, particularly in regenerative medicine and tissue engineering. By generating COL12 as a recombinant protein, scientists aim to elucidate its mechanistic pathways, enabling the development of targeted approaches for diseases associated with collagen dysregulation. The exploration of COL12 not only enhances our understanding of collagen biology but also opens new avenues for innovative treatments based on ECM modulation.
