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1000 results found for “ghrp”
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Name :
GPT HumanDescription:
Glutamic-Pyruvate Transaminase Human Recombinant
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
Product # :
ENZ-192Price :
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Shipped with Ice Packs
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Description
GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
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Synonyms
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
M6PR HumanDescription:
Mannose-6-Phosphate Receptor Human Recombinant
Mannose-6-Phosphate Receptor (Cation Dependent), CD-MPR, MPR46, CD Man-6-P Receptor, MPR 46, 46-KDa Mannose 6-Phosphate Receptor, MPR-46, SMPR, Cation-Dependent Mannose-6-Phosphate Receptor, Mr 46,000 Man6PR, Small Mannose 6-Phosphate Receptor, 46 KDa Mannose 6-Phosphate Receptor, MPRD, M6PR.
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PRO-1961Price :
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Description
M6PR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (27-185) and having a molecular mass of 20.3kDa.M6PR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The M6PR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Mannose-6-Phosphate Receptor (M6PR) belongs to the P-type lectin family. P-type lectins play a vital role in lysosome function through the specific transport of mannose-6-phosphate-containing acid hydrolases from the Golgi complex to lysosomes. The M6PR protein functions as a homodimer and needs divalent cations for ligand binding. Lysosomal enzymes carrying phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the ensuing receptor-ligand complex is transferred to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.
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Synonyms
Mannose-6-Phosphate Receptor (Cation Dependent), CD-MPR, MPR46, CD Man-6-P Receptor, MPR 46, 46-KDa Mannose 6-Phosphate Receptor, MPR-46, SMPR, Cation-Dependent Mannose-6-Phosphate Receptor, Mr 46,000 Man6PR, Small Mannose 6-Phosphate Receptor, 46 KDa Mannose 6-Phosphate Receptor, MPRD, M6PR.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTEEKTCD LVGEKGKESE KELALVKRLK PLFNKSFEST VGQGSDTYIY IFRVCREAGN HTSGAGLVQI NKSNGKETVV GRLNETHIFN GSNWIMLIYK GGDEYDNHCG KEQRRAVVMI SCNRHTLADN FNPVSEERGK VQDCFYLFEM DSSLACSPEI SH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VEGFR2 Human, HisDescription:
Vascular Endothelial Growth Factor receptor-2 Human Recombinant, His Tag
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Product # :
PKA-099Price :
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Description
VEGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 987 amino acids (20-764a.a) and having a molecular mass of 110.5kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). VEGFR2 is fused to a 239 amino acids hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
VEGFR2 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. -
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPASVGLPS VSLDLPRLSI QKDILTIKAN TTLQITCRGQ RDLDWLWPNN QSGSEQRVEV TECSDGLFCK TLTIPKVIGN DTGAYKCFYR ETDLASVIYV YVQDYRSPFI ASVSDQHGVV YITENKNKTV VIPCLGSISN LNVSLCARYP EKRFVPDGNR ISWDSKKGFT IPSYMISYAG MVFCEAKIND ESYQSIMYIV VVVGYRIYDV VLSPSHGIEL SVGEKLVLNC TARTELNVGI DFNWEYPSSK HQHKKLVNRD LKTQSGSEMK KFLSTLTIDG VTRSDQGLYT CAASSGLMTK KNSTFVRVHE KPFVAFGSGM ESLVEATVGE RVRIPAKYLG YPPPEIKWYK NGIPLESNHT IKAGHVLTIM EVSERDTGNY TVILTNPISK EKQSHVVSLV VYVPPQIGEK SLISPVDSYQ YGTTQTLTCT VYAIPPPHHI HWYWQLEEEC ANEPSQAVSV TNPYPCEEWR SVEDFQGGNK IEVNKNQFAL IEGKNKTVST LVIQAANVSA LYKCEAVNKV GRGERVISFH VTRGPEITLQ PDMQPTEQES VSLWCTADRS TFENLTWYKL GPQPLPIHVG ELPTPVCKNL DTLWKLNATM FSNSTNDILI MELKNASLQD QGDYVCLAQD RKTKKRHCVV RQLTVLERVA PTITGNLENQ TTSIGESIEV SCTASGNPPP QIMWFKDNET LVEDSGIVLK DGNRNLTIRR VRKEDEGLYT CQACSVLGCA KVEAFFIIEG AQEKTNLELE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HARS Human, HisDescription:
Histidyl-tRNA Synthetase Human Recombinant, His Tag
Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.
Product # :
ENZ-001Price :
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Shipped with Ice Packs
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Description
HARS Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 532 amino acids (1-509 a.a.) and having a molecular mass of 59.4kDa. The HARS is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HARS solution (1mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol,
1mM DTT and 0.1M NaCl.Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Histidyl-tRNA synthetase (HARS) functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids. HARS is a member of the class II family of aminoacyl-tRNA synthetases. HARS is responsible for the synthesis of histidyl-transfer RNA, which is vital for the incorporation of histidine into proteins. HARS is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
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Synonyms
Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAERAAL EELVKLQGER VRGLKQQKAS AELIEEEVAK LLKLKAQLGP DESKQKFVLK TPKGTRDYSP RQMAVREKVF DVIIRCFKRH GAEVIDTPVF ELKETLMGKY GEDSKLIYDL KDQGGELLSL RYDLTVPFAR YLAMNKLTNI KRYHIAKVYR RDNPAMTRGR YREFYQCDFD IAGNFDPMIP DAECLKIMCE ILSSLQIGDF LVKVNDRRIL DGMFAICGVS DSKFRTICSS VDKLDKVSWE EVKNEMVGEK GLAPEVADRI GDYVQQHGGV SLVEQLLQDP KLSQNKQALE GLGDLKLLFE YLTLFGIDDK ISFDLSLARG LDYYTGVIYE AVLLQTPAQA GEEPLGVGSV AAGGRYDGLV GMFDPKGRKV PCVGLSIGVE RIFSIVEQRL EALEEKIRTT ETQVLVASAQ KKLLEERLKL VSELWDAGIK AELLYKKNPK LLNQLQYCEE AGIPLVAIIG EQELKDGVIK LRSVTSREEV DVRREDLVEE IKRRTGQPLC IC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description:
Human Follicle Stimulating Hormone
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
Product # :
HOR-249Price :
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Shipped at Room temp
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Description
FSH Human is a glycoprotein produced from urine of post-menopausal women and having a total molecular mass of 30,000 Dalton.FSH is a heterodimeric hormone consisting of 92 amino acids a chain and 111 amino acids b chain.The FSH is purified by proprietary chromatographic techniques.
Source
Urine of post-menopausal women.
Formulation
The FSH was lyophilized with no additives.
Citations
More Info
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Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproductionIn women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production.
In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis.
In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle.
Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone(GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads. -
Synonyms
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH-beta should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Follicle Stimulating Hormone in sterile pyrogen free water at 2,000IU/1ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of FOLLICLE STIMULATING HORMONE HUMAN Protein?
FOLLICLE STIMULATING HORMONE HUMAN Protein has a total Mw of 30kDa.
What is the source or expression system of FOLLICLE STIMULATING HORMONE HUMAN Protein?
Urine of post-menopausal women.
What is the Biological Activity of FOLLICLE STIMULATING HORMONE HUMAN Protein?
The biological functionality of FOLLICLE STIMULATING HORMONE HUMAN Protein will be determined in the future.
What is the amino acid sequence of FOLLICLE STIMULATING HORMONE HUMAN Protein?
FOLLICLE STIMULATING HORMONE HUMAN Protein is composed from 92 amino acids a chain and 111 amino acids b chain.
What applications can FOLLICLE STIMULATING HORMONE HUMAN Protein be used in?
FOLLICLE STIMULATING HORMONE HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLICLE STIMULATING HORMONE HUMAN Protein?
The endotoxin level is minimal, FOLLICLE STIMULATING HORMONE HUMAN Protein was purified using conventional chromatography techniques.
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Contaminants
Less than: 0.1% hCG, 0.5%TSH, 0.5% LH, 0.5%GH and 0.5%Prl.Free of HbsAg, antibodies to HIV and HCV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FABP3 Human, NativeDescription:
Fatty Acid Binding Protein-3 Human, Native
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
Product # :
PRO-2794Price :
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Description
FABP3 Human produced in Human cardiac muscle tissue having a molecular mass of 15kDa and is purified by proprietary chromatographic technique.
Source
Human heart tissue.
Formulation
FABP3 was lyophilized from 10mM Tris-HCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fatty Acid Binding Protein-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized FABP3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
FABP3 is abundantly expressed in cardiac and skeletal muscle tissues, where it serves as a crucial mediator in the cellular handling of fatty acids. By facilitating the uptake, transport, and utilization of fatty acids, FABP3 ensures a steady supply of energy, making it indispensable for the high-energy-demanding heart and skeletal muscles. Beyond its role in energy metabolism, FABP3 has been implicated in diverse cellular processes, including inflammation, oxidative stress response, and cellular differentiation.
Molecular Insights:
At the molecular level, FABP3 exhibits a remarkable affinity for long-chain fatty acids. Its unique binding properties enable it to shuttle fatty acids to specific cellular compartments, such as mitochondria, for β-oxidation. Additionally, FABP3 is intricately involved in the regulation of gene expression, modulating the activity of various transcription factors and signaling pathways. Understanding these molecular intricacies is key to deciphering FABP3's diverse functions.
Physiological Significance:
In cardiac muscle, FABP3 plays a crucial role in myocardial energy metabolism. During periods of increased energy demand, such as cardiac stress or exercise, FABP3 ensures a rapid supply of fatty acids for ATP production. Its absence or dysfunction has been associated with impaired cardiac function and increased susceptibility to ischemic injury. In skeletal muscles, FABP3 contributes to the utilization of fatty acids as an energy source during sustained physical activity.
Implications in Disease:
Research indicates that alterations in FABP3 expression and function are linked to several pathological conditions. In cardiovascular diseases, FABP3 has emerged as a potential biomarker for myocardial infarction, reflecting myocardial damage. Moreover, studies have highlighted its involvement in insulin resistance, diabetes, and metabolic syndrome, emphasizing its significance in metabolic disorders.
Therapeutic Prospects:
The unique properties of FABP3 have garnered attention in drug development. Researchers are exploring FABP3-targeted therapies for cardiovascular diseases and metabolic disorders. Modulating FABP3 activity presents a promising avenue for managing conditions characterized by dysregulated fatty acid metabolism and oxidative stress.
Conclusion:
FABP3, the unassuming intracellular fatty acid chaperone, plays a central role in human physiology and disease. Its intricate involvement in energy metabolism, cellular signaling, and disease pathogenesis underscores its significance as a research subject. As our understanding of FABP3 deepens, it opens doors to innovative diagnostic approaches and therapeutic interventions, potentially impacting millions of lives worldwide.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
hchA E.ColiDescription:
Chaperone Protein hchA E.Coli Recombinant
Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.
Product # :
HSP-043Price :
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Description
hchA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-283 a.a.) and having a molecular mass of 33.3kDa.hchA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The hchA contains (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Escherichia coli Hsp31 (HchA) is a homodimeric member of the ThiI/DJ-1/PfpI superfamily which combines molecular chaperone and aminopeptidase activities. HchA uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress.
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Synonyms
Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
hchA E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HERC5 HumanDescription:
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant
HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.
Product # :
ENZ-797Price :
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Description
HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.
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Synonyms
HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NDRG2 HumanDescription:
N-Myc Downstream Regulated 2 Human Recombinant
N-myc downstream-regulated gene 2 protein, NDR1-related protein NDR2, protein NDRG2, NDRG family member 2, cytoplasmic protein Ndr1, syld709613 protein, KIAA1248, SYLD.
Product # :
PRO-1198Price :
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Description
NDRG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 41.8 kDa.NDRG2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NDRG2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NDRG2 belongs to the N-myc downregulated gene family that is a part of the alpha/beta hydrolase superfamily. NDRG2 takes part in dendritic and neuronal cell differentiation and outgrowth and is found in large quantities in heart, dendritic cells, brain, salivary gland and skeletal muscle and in small quantities in kidney and liver. In Alzheimer Disease (AD)-affected patients NDRG2 is found in brain lesions and is believed to be related to the progression of AD.
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Synonyms
N-myc downstream-regulated gene 2 protein, NDR1-related protein NDR2, protein NDRG2, NDRG family member 2, cytoplasmic protein Ndr1, syld709613 protein, KIAA1248, SYLD.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAELQE VQITEEKPLL PGQTPEAAKT HSVETPYGSV TFTVYGTPKP KRPAILTYHD VGLNYKSCFQ PLFQFEDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS LDQLADMIPC VLQYLNFSTI IGVGVGAGAY ILARYALNHP DTVEGLVLIN IDPNAKGWMD WAAHKLTGLT SSIPEMILGH LFSQEELSGN SELIQKYRNI ITHAPNLDNI ELYWNSYNNR RDLNFERGGD ITLRCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASVD GNRSRSRTLS QSSESGTLSS GPPGHTMEVS C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ARPP19 HumanDescription:
CAMP-Regulated Phosphoprotein, 19kDa Human Recombinant
CAMP-Regulated Phosphoprotein 19kDa, ARPP-19, ARPP16, Endosulfine Alpha-Like, ARPP-16, ENSAL, CAMP-Regulated Phosphoprotein 19, Cyclic AMP Phosphoprotein 19 KD, ARPP19.
Product # :
PRO-1785Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARPP19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (1-112 a.a) and having a molecular mass of 14.7kDa.ARPP19 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARPP19 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
cAMP-regulated phosphoprotein 19 (ARPP19) is protein phosphatase inhibitor which specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, ARPP19 specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, a vital condition to maintain cyclin-B1-CDK1 activity high during M phase. ARPP19 protein may indirectly boost GAP-43 expression. The 19 kDa cAMP-regulated phosphoprotein has a role in regulating mitosis by obstructing protein phosphatase-2A.
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Synonyms
CAMP-Regulated Phosphoprotein 19kDa, ARPP-19, ARPP16, Endosulfine Alpha-Like, ARPP-16, ENSAL, CAMP-Regulated Phosphoprotein 19, Cyclic AMP Phosphoprotein 19 KD, ARPP19.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAEVPE AASAEEQKEM EDKVTSPEKA EEAKLKARYP HLGQKPGGSD FLRKRLQKGQ KYFDSGDYNM AKAKMKNKQL PTAAPDKTEV TGDHIPTPQD LPQRKPSLVA SKLAG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ASPH HumanDescription:
Aspartate Beta-Hydroxylase Human Recombinant
AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.
Product # :
ENZ-488Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (75-270 a.a.) and having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.
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Synonyms
AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNX3 HumanDescription:
Sorting Nexin 3 Human Recombinant
Sorting nexin-3, Protein SDP3, SNX3, SDP3, Grd19, MCOPS8.
Product # :
PRO-246Price :
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Shipping Method :
Shipped with Ice Packs
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Description
SNX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-162 a.a) and having a molecular mass of 20.9kDa.SNX3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNX3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Sorting nexin 3 (SNX3) belongs to the large family of hydrophilic proteins, which interact with various receptor types and are involved in intracellular trafficking. SNX3 interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. SNX3 comprises a distinct subgroup of nexins, which share less sequence similarity outside of the PX domain and have significantly different binding affinities for the tyrosine kinase receptors.
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Synonyms
Sorting nexin-3, Protein SDP3, SNX3, SDP3, Grd19, MCOPS8.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
SNX3 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR
HA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EGFPDescription:
Enhanced Green Fluorescent Protein Recombinant
Green fluorescent protein, GFP.
Product # :
PRO-1606Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGFP was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
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Synonyms
Green fluorescent protein, GFP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BMP 7 Human, HisDescription:
Bone Morphogenetic Protein-7 Human Recombinant, His Tag
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Product # :
CYT-629Price :
Quantity :
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Description
BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
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Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.
What is the source or expression system of BMP7 Protein?
Escherichia Coli.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.
What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FABP6 Human, HisDescription:
Fatty Acid Binding Protein 6 Human Recombinant, His Tag
I-BABP, ILBP, I-15P, I-BAP, ILBP3, ILLBP, I-BABP, I-BALB, FABP-6, Gastrotropin, Ileal lipid-binding protein, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, Fatty acid-binding protein 6, FABP6.
Product # :
PRO-667Price :
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Description
FABP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids and having a molecular mass of 18 kDa. FABP6 is fused to His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP6 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FABP6 also called ileal fatty acid binding protein, is part of the small family of highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP6 cytosolic protein binds bile acid. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. Alternate transcription promoters generate 2 transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is acetylated on Ala2. FABP6 binds together fatty acids and bile acids and is directly involved in fatty acid transport and metabolism.
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Synonyms
I-BABP, ILBP, I-15P, I-BAP, ILBP3, ILLBP, I-BABP, I-BALB, FABP-6, Gastrotropin, Ileal lipid-binding protein, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, Fatty acid-binding protein 6, FABP6.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
THAP7 HumanDescription:
THAP Domain Containing, Apoptosis Associated Protein 7 Human Recombinant
THAP domain containing 7, THAP7.
Product # :
PRO-1989Price :
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Shipping Method :
Shipped with Ice Packs
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Description
THAP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.8kDa. THAP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
THAP7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
THAP Domain Containing, Apoptosis Associated Protein 7 (THAP7) holds one THAP-type zinc finger. THAP7 is a chromatin-associated, histone tail-binding protein which represses transcription by recruiting HDAC3 and nuclear hormone receptor corepressors.
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Synonyms
THAP domain containing 7, THAP7.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPRHCSA AGCCTRDTRE TRNRGISFHR LPKKDNPRRG LWLANCQRLD PSGQGLWDPA SEYIYFCSKH FEEDCFELVG ISGYHRLKEG AVPTIFESFS KLRRTTKTKG HSYPPGPAEV SRLRRCRKRC SEGRGPTTPF SPPPPADVTC FPVEEASAPA TLPASPAGRL EPGLSSPFSD LLGPLGAQAD EAGCSAQPSP ERQPSPLEPR PVSPSAYMLR LPPPAGAYIQ NEHSYQVGSA LLWKRRAEAA LDALDKAQRQ LQACKRREQR LRLRLTKLQQ ERAREKRAQA DARQTLKEHV QDFAMQLSSS MA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PIR HumanDescription:
Pirin Human Recombinant
Pirin, Probable quercetin 2,3-dioxygenase PIR, Probable quercetinase, PIR.
Product # :
PRO-1040Price :
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Description
PIR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-290 a.a.) and having a molecular mass of 34.3kDa.PIR is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Pirin (PIR) which belongs to the cupin superfamily, is an Fe(II)-containing nuclear protein expressed in all tissues of the body and concentrated within dot-like subnuclear structures. Pirin may function as a transcriptional cofactor and is involved in the regulation of DNA transcription and replication, as a result of interactions with nuclear factor I/CCAAT box transcription factor as well as B cell lymphoma 3-encoded oncoprotein.
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Synonyms
Pirin, Probable quercetin 2,3-dioxygenase PIR, Probable quercetinase, PIR.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGRP GGFPDHPHRG FETVSYLLEG GSMAHEDFCG HTGKMNPGDL QWMTAGRGIL HAEMPCSEEP AHGLQLWVNL RSSEKMVEPQ YQELKSEEIP KPSKDGVTVA VISGEALGIK SKVYTRTPTL YLDFKLDPGA KHSQPIPKGW TSFIYTISGD VYIGPDDAQQ KIEPHHTAVL GEGDSVQVEN KDPKRSHFVL IAGEPLREPV IQHGPFVMNT NEEISQAILD FRNAKNGFER AKTWKSKIGN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GET4 HumanDescription:
Golgi To ER Traffic Protein 4 Human Recombinant
Golgi to ER traffic protein 4 homolog (S. cerevisiae), C7orf20, CEE, CGI-20, TRC35, Golgi to ER traffic protein 4 homolog, Conserved edge-expressed protein, Transmembrane domain recognition complex 35 kDa subunit, GET4.
Product # :
PRO-1868Price :
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Description
GET4 Human Recombinant produced in E. coli is. a single polypeptide chain containing 350 amino acids (1-327) and having a molecular mass of 38.9kDa. GET4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GET4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BAT3 complex is a multiprotein complex which takes part in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. Golgi To ER Traffic Protein 4 (GET4) is a part of the BAT3 complex. The complex functions by helping TA proteins (which contain a single C-terminal transmembrane region) which are captured by ASNA1/TRC40. BAT3 complex synthesizes membrane proteins, interacts with the transmembrane area of recently released TA proteins, and transfers them to ASNA1/TRC40 for targeting.
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Synonyms
Golgi to ER traffic protein 4 homolog (S. cerevisiae), C7orf20, CEE, CGI-20, TRC35, Golgi to ER traffic protein 4 homolog, Conserved edge-expressed protein, Transmembrane domain recognition complex 35 kDa subunit, GET4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAAAAM AEQESARNGG RNRGGVQRVE GKLRASVEKG DYYEAHQMYR TLFFRYMSQS KHTEARELMY SGALLFFSHG QQNSAADLSM LVLESLEKAE VEVADELLEN LAKVFSLMDP NSPERVTFVS RALKWSSGGS GKLGHPRLHQ LLALTLWKEQ NYCESRYHFL HSADGEGCAN MLVEYSTSRG FRSEVDMFVA QAVLQFLCLK NKSSASVVFT TYTQKHPSIE DGPPFVEPLL NFIWFLLLAV DGGKLTVFTV LCEQYQPSLR RDPMYNEYLD RIGQLFFGVP PKQTSSYGGL LGNLLTSLMG SSEQEDGEES PSDGSPIELD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL3 MouseDescription:
GRO-Gamma Mouse Recombinant (CXCL3)
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960.
Product # :
CHM-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO-g Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7.7kDa. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse CXCL3 lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.Citations
More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GRO-gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SELRCQCLNT LPRVDFETIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QGPRLQIIIK KILKSGKSS.
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Background
What is the molecular weight/Mw of CXCL3 MOUSE Protein?
CXCL3 MOUSE Protein has a total Mw of 7.7kDa.
What is the source or expression system of CXCL3 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL3 MOUSE Protein?
CXCL3 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 MOUSE Protein?
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.
What is the amino acid sequence of CXCL3 MOUSE Protein?
SELRCQCLNT LPRVDFETIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QGPRLQIIIK KILKSGKSS.
What applications can CXCL3 MOUSE Protein be used in?
CXCL3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 MOUSE Protein?
The endotoxin level is minimal, CXCL3 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL3 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL3 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RANBP3 HumanDescription:
RAN Binding Protein 3 Human Recombinant
RAN binding protein 3, RanBP3.
Product # :
PRO-1986Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RANBP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (235-445 a.a) and having a molecular mass of 25.5kDa. RANBP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RANBP3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RAN Binding Protein 3, also known as RANBP3, is found in the nucleus and cytoplasm. RANBP3 which owns RanBD1 domain participates in nuclear export as part of a heteromeric complex. RANBP3 is also negatively regulates TGF-beta signaling by interacting with the R-SMAD proteins, SMAD2 and SMAD3.
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Synonyms
RAN binding protein 3, RanBP3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSISSSLEN STNSADASSN KFVFGQNMSE RVLSPPKLNE VSSDANRENA AAESGSESSS QEATPEKESL AESAAAYTKA TARKCLLEKV EVITGEEAES NVLQMQCKLF VFDKTSQSWV ERGRGLLRLN DMASTDDGTL QSRLVMRTQG SLRLILNTKL WAQMQIDKAS EKSIRITAMD TEDQGVKVFL ISASSKDTGQ LYAALHHRIL ALRS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GDF7 MouseDescription:
Growth and Differentiation factor 7 Mouse Recombinant
Growth/differentiation factor 7, GDF-7, Gdf7.
Product # :
CYT-946Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF7 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 146 amino acids and having a molecular mass of 29.8kDa.The GDF-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF7 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.Citations
More Info
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Introduction
Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.
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Synonyms
Growth/differentiation factor 7, GDF-7, Gdf7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.
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Background
What is the molecular weight/Mw of GDF7 Protein?
GDF7 Protein has a total Mw of 29.8kDa.
What is the source or expression system of GDF7 Protein?
Escherichia Coli.
What is the Purity of GDF7 Protein?
GDF7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF7 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.
What is the amino acid sequence of GDF7 Protein?
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.
What applications can GDF7 Protein be used in?
GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF7 Protein?
The endotoxin level is minimal, GDF7 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A8 Human, HisDescription:
S100 Calcium Binding Protein A8 Human Recombinant, His Tag
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-150Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100A8 was filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris and 100mM NaCl, pH 7.5.
Citations
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQEMLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HN1 HumanDescription:
Hematological And Neurological Expressed 1 Human Recombinant
ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.
Product # :
PRO-1434Price :
Quantity :
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Shipped with Ice Packs
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Description
HN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 18.1kDa. HN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HN1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hematological and neurological expressed 1 protein (HN1) is a small protein which is extremely preserved among species. HN1 expression is upregulated in regenerating neural tissues, including the axotomized adult rodent facial motor nerve and dedifferentiating retinal pigment epithelial cells of the Japanese newt. HN1 is also expressed in several tissues during embryonic development as well as in regions of the adult brain which display high plasticity.
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Synonyms
ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN IFGTPEENQA SWAKSAGAKS SGGREDLESS GLQRRNSSEA SSGDFLDLKG EGDIHENVDT DLPGSLGQSE EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.