Analytical Data
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基因名
TNX
- Application
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别名
TNX；HXBL；TNX；TNXB1；Tenascin-X
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P22105
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表达区间
1-673aa
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氨基酸序列
MRLSWSVAQGPFDSFVVQYEDTNGQPQALLVDGDQSKILISGLEPSTPYRFLLYGLHEGK RLGPLSAEGTTGLAPAGQTSEESRPRLSQLSVTDVTTSSLRLNWEAPPGAFDSFLLRFGV PSPSTLEPHPRPLLQRELMVPGTRHSAVLRDLRSGTLYSLTLYGLRGPHKADSIQGTART LSPVLESPRDLQFSEIRETSAKVNWMPPPSRADSFKVSYQLADGGEPQSVQVDGQARTQK LQGLIPGARYEVTVVSVRGFEESEPLTGFLTTVPDGPTQLRALNLTEGFAVLHWKPPQNP VDTYDVQVTAPGAPPLQAETPGSAVDYPLHDLVLHTNYTATVRGLRGPNLTSPASITFTT GLEAPRDLEAKEVTPRTALLTWTEPPVRPAGYLLSFHTPGGQNQEILLPGGITSHQLLGL FPSTSYNARLQAMWGQSLLPPVSTSFTTGGLRIPFPRDCGEEMQNGAGASRTSTIFLNGN RERPLNVFCDMETDGGGWLVFQRRMDGQTDFWRDWEDYAHGFGNISGEFWLGNEALHSLT QAGDYSMRVDLRAGDEAVFAQYDSFHVDSAAEYYRLHLEGYHGTAGDSMSYHSGSVFSAR DRDPNSLLISCAVSYRGAWWYRNCHYANLNGLYGSTVDHQGVSWYHWKGFEFSVPFTEMK LRPRNFRSPAGGG
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
The TNX (Tendon extracellularmatrix protein) recombinant protein research dates back to the increasing interest in understanding the molecular mechanisms of tendon biology and pathology. Tendons play a crucial role in musculoskeletal health, serving as the connection between muscles and bones, yet their healing processes are often slow and complicated, particularly in the context of injuries and degenerative diseases. TNX has been identified as a vital component of the extracellular matrix (ECM) in tendons, influencing cell behavior, tissue organization, and mechanical properties. Researchers have sought to explore TNX's specific functions and interactions within the ECM, leading to its production as a recombinant protein for further investigation. This synthetic version allows for detailed biochemical analysis and functional studies, including assessments of its role in tendon cell proliferation, migration, and differentiation. The advancement of recombinant DNA technology has facilitated the production of TNX in a controlled environment, enabling researchers to isolate its effects and evaluate potential therapeutic applications. Given the high incidence of tendon injuries and the limitations of current treatment strategies, understanding TNX's role could pave the way for novel regenerative therapies aimed at enhancing tendon repair and function. Thus, TNX recombinant protein research is positioned at the intersection of molecular biology and clinical application, with the potential to significantly impact tendon health and rehabilitation strategies.
