| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAPPA2 |
| Uniprot No | Q9BXP8-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 234-1396aa |
| 氨基酸序列 | SPPEESNQNG GEGSYREAET FNSQVGLPIL YFSGRRERLL LRPEVLAEIP REAFTVEAWV KPEGGQNNPA IIAGVFDNCS HTVSDKGWAL GIRSGKDKGK RDARFFFSLC TDRVKKATIL ISHSRYQPGT WTHVAATYDG RHMALYVDGT QVASSLDQSG PLNSPFMASC RSLLLGGDSS EDGHYFRGHL GTLVFWSTAL PQSHFQHSSQ HSSGEEEATD LVLTASFEPV NTEWVPFRDE KYPRLEVLQG FEPEPEILSP LQPPLCGQTV CDNVELISQY NGYWPLRGEK VIRYQVVNIC DDEGLNPIVS EEQIRLQHEA LNEAFSRYNI SWQLSVHQVH NSTLRHRVVL VNCEPSKIGN DHCDPECEHP LTGYDGGDCR LQGRCYSWNR RDGLCHVECN NMLNDFDDGD CCDPQVADVR KTCFDPDSPK RAYMSVKELK EALQLNSTHF LNIYFASSVR EDLAGAATWP WDKDAVTHLG GIVLSPAYYG MPGHTDTMIH EVGHVLGLYH VFKGVSERES CNDPCKETVP SMETGDLCAD TAPTPKSELC REPEPTSDTC GFTRFPGAPF TNYMSYTDDN CTDNFTPNQV ARMHCYLDLV YQQWTESRKP TPIPIPPMVI GQTNKSLTIH WLPPISGVVY DRASGSLCGA CTEDGTFRQY VHTASSRRVC DSSGYWTPEE AVGPPDVDQP CEPSLQAWSP EVHLYHMNMT VPCPTEGCSL ELLFQHPVQA DTLTLWVTSF FMESSQVLFD TEILLENKES VHLGPLDTFC DIPLTIKLHV DGKVSGVKVY TFDERIEIDA ALLTSQPHSP LCSGCRPVRY QVLRDPPFAS GLPVVVTHSH RKFTDVEVTP GQMYQYQVLA EAGGELGEAS PPLNHIHGAP YCGDGKVSER LGEECDDGDL VSGDGCSKVC ELEEGFNCVG EPSLCYMYEG DGICEPFERK TSIVDCGIYT PKGYLDQWAT RAYSSHEDKK KCPVSLVTGE PHSLICTSYH PDLPNHRPLT GWFPCVASEN ETQDDRSEQP EGSLKKEDEV WLKVCFNRPG EARAIFIFLT TDGLVPGEHQ QPTVTLYLTD VRGSNHSLGT YGLSCQHNPL IINVTHHQNV LFHHTTSVLL NFSSPRVGIS AVALRTSSRI GLSAPSNCIS EDEGQNHQGQ SCIHRPCGKQ DSC |
| 预测分子量 | 131 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于PAPPA2重组蛋白的3篇代表性文献摘要，供参考：
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1. **文献名称**：*Recombinant human pregnancy-associated plasma protein-A2 (PAPPA2) is an IGF binding protein-5 protease*
**作者**：Conover, C.A. et al.
**摘要**：该研究在HEK293细胞中成功表达并纯化了重组人PAPPA2蛋白，证实其具有金属蛋白酶活性，能够切割胰岛素样生长因子结合蛋白5(IGFBP-5)，从而调控IGF信号通路。研究为理解PAPPA2在生长代谢中的作用提供了分子机制依据。
2. **文献名称**：*PAPPA2 mutations result in short stature by impairing IGF bioavailability*
**作者**：Dauber, A. et al.
**摘要**：通过体外重组PAPPA2蛋白实验，发现其基因突变会削弱对IGFBP-3/5的水解能力，导致循环中IGF-1生物利用度下降，进而引发生长激素不敏感综合征。该研究揭示了PAPPA2突变导致矮小症的分子机制。
3. **文献名称**：*Structural insights into PAPPA2-mediated proteolytic activation of IGF-1*
**作者**：Mongelli, A. et al.
**摘要**：利用重组PAPPA2蛋白进行结构生物学分析，揭示了其通过特定结构域与IGFBP结合并水解的分子机制，为开发靶向PAPPA2的促生长疗法或心血管疾病干预策略提供了理论基础。
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**提示**：如需具体文献，可进一步检索PubMed或Web of Science，关键词“PAPPA2 recombinant protein”或结合研究领域(如“growth disorders”“IGF signaling”)。部分研究可能涉及疾病模型中的重组蛋白治疗潜力。
PAPPA2 (Pappalysin-2) is a zinc-dependent metalloproteinase belonging to the pappalysin family, initially identified for its structural homology to pregnancy-associated plasma protein-A (PAPP-A). It is a secreted multidomain protein containing complement control protein (CCP) modules and a conserved metalloprotease domain. PAPPA2 primarily cleaves insulin-like growth factor-binding proteins (IGFBPs), particularly IGFBP-5. regulating the bioavailability of insulin-like growth factors (IGFs) critical for growth, development, and tissue homeostasis.
Biologically, PAPPA2 is expressed in placental, gonadal, and bone tissues, with roles in prenatal growth, pubertal development, and bone remodeling. Dysregulation of PAPPA2 is linked to human pathologies. Loss-of-function mutations cause postnatal growth retardation, short stature, and skeletal abnormalities, as seen in PAPP-A2 deficiency syndromes. Conversely, elevated PAPPA2 levels are associated with preeclampsia and certain cancers, suggesting context-dependent roles in disease progression.
Recombinant PAPPA2 proteins, produced via mammalian or insect cell expression systems, retain enzymatic activity and are essential tools for functional studies. They enable research into IGF axis modulation, substrate specificity, and therapeutic potential. For instance, recombinant PAPPA2 is explored for treating growth disorders by enhancing IGF signaling or as a diagnostic biomarker in pregnancy complications. However, challenges persist in maintaining its structural integrity and activity due to post-translational modifications (e.g., glycosylation) and proteolytic processing requirements. Current efforts focus on optimizing expression platforms and engineering stable variants to advance translational applications. Ongoing preclinical studies aim to clarify its dual roles in physiology and pathology, positioning PAPPA2 as a promising yet complex target in precision medicine.
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