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1000 results found for “Cysteine-Rich Secretory Protein”
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Name :
CRP Human RecombinantDescription:
c-Reactive Protein Human Recombinant
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Product # :
PRO-335Price :
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Shipped with Ice Packs
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- sds-page
Description
Recombinant Human CRP produced in E.Coli is a non-glycosylated polypeptide chain having a total molecular mass of 115 kDa that corresponds to the pentamer structure of 23 kDa monomer determined by amino acid sequence. The CRP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile protein solution contains 20mM Tris (pH 7.5), 2mM CaCl2, 0.14M NaCl and 0.05% NaN3.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
sds-page
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CRP should be stored at all times at 4°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.
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Name :
CCDC25 HumanDescription:
Coiled-Coil Domain Containing 25 Human Recombinant
Coiled-coil domain-containing protein 25, CCDC25.
Product # :
PRO-1655Price :
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Description
CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.
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Synonyms
Coiled-coil domain-containing protein 25, CCDC25.
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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 MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.
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 :
VPS28 HumanDescription:
Vacuolar Protein Sorting 28 Human Recombinant
Vacuolar protein sorting-associated protein 28 homolog, ESCRT-I complex subunit VPS28, H-Vps28, VPS28, MGC60323.
Product # :
PRO-730Price :
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Description
VPS28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-221 a.a.) and having a molecular mass of 25.4kDa.The VPS28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VPS28 protein solution contains 20mM Tris-HCl buffer (pH 7.5), 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
VPS28 is a subunit of the ESCRT-I complex (endosomal complexes required for transport) involved in the sorting of ubiquitinated proteins. VPS28 is involved in endosomal sorting of cell surface receptors using a multivesicular body/late endosome pathway. VSP28 binding with the TSG101 may have significant roles in budding of Retroviruses, such as HIV-1 and Ebola virus.
VSP28 interacts with TSG101, VPS37B, VPS37C, FAM125A and FAM125B, and also with VPS36, this interaction mediates the association with the ESCRT-II complex. Furthermore it interacts with SNF8 and VPS25 and CEP55. -
Synonyms
Vacuolar protein sorting-associated protein 28 homolog, ESCRT-I complex subunit VPS28, H-Vps28, VPS28, MGC60323.
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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
MFHGIPATPG IGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC VSPSEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A.
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 :
WHSC2 HumanDescription:
Wolf-Hirschhorn Syndrome Candidate 2 Human Recombinant
Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.
Product # :
PRO-062Price :
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Description
WHSC2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 559 amino acids (1-539 a.a.) and having a molecular mass of 60.6kDa. The WHSC2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WHSC2 solution (0.25 mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
WHSC2 (NELF-A) is a protein factor required for DRB-sensitive transcription. WHSC2 is one of the 5 components of the multisubunit NELF complex which cooperates with DSIF to repress RNA polymerase II elongation. The Wolf-Hirschhorn syndrome is a multiple malformation syndrome characterized by mental and developmental defects resulting from a hemizygous deletion of the distal short arm of chromosome 4 (4p16.3).
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Synonyms
Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.
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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 MPGQRRALSP KMASMRESDT GLWLHNKLGA TDELWAPPSI ASLLTAAVID NIRLCFHGLS SAVKLKLLLG TLHLPRRTVD EMKGALMEII QLASLDSDPW VLMVADILKS FPDTGSLNLE LEEQNPNVQD ILGELREKVG ECEASAMLPL ECQYLNKNAL TTLAGPLTPP VKHFQLKRKP KSATLRAELL QKSTETAQQL KRSAGVPFHA KGRGLLRKMD TTTPLKGIPK QAPFRSPTAP SVFSPTGNRT PIPPSRTLLR KERGVKLLDI SELDMVGAGR EAKRRRKTLD AEVVEKPAKE ETVVENATPD YAAGLVSTQK LGSLNNEPAL PSTSYLPSTP SVVPASSYIP SSETPPAPSS REASRPPEEP SAPSPTLPAQ FKQRAPMYNS GLSPATPTPA APTSPLTPTT PPAVAPTTQT PPVAMVAPQT QAPAQQQPKK NLSLTREQMF AAQEMFKTAN KVTRPEKALI LGFMAGSREN PCQEQGDVIQ IKLSEHTEDL PKADGQGSTT MLVDTVFEMN YATGQWTRFK KYKPMTNVS.
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 :
Protein-G HisDescription:
Protein G His Tag Recombinant
Product # :
PRO-1237Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Protein G His Tag Recombinant produced in E.Coli is a 201 amino acids protein which contains amino acid 190-384 of the Streptococcus sp with a C-terminal 6-His tag, and having a molecular mass of 21.6kDa. But it migrates with an apparent molecular mass of 32kDa in SDS-PAGE.The Protein G His Tag is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein G binds to the constant region of many species of immunoglobulin G. It can be used to detect, quantify and purify IgG antibodies and antibody/antigen complexes. Recombinant Protein G contains only IgG binding domains. The albumin-binding domain as well as cell wall and cell membrane binding domains have been removed to ensure the maximum specific IgG binding capacity.
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Specificity
1. Binds with greater affinity to most mammalian immunoglobulins than Protein A, including human IgG3 and rat IgG2a.2. Does not bind to human IgM, IgD and IgA.
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 :
GREM2 HumanDescription:
GREM2 Human Recombinant
CKTSF1B2, DAND3, PRDC, Gremlin-2, Cysteine knot superfamily 1, BMP antagonist 2, DAN domain family member 3, Protein related to DAN and cerberus, GREM2.
Product # :
PRO-1428Price :
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Description
GREM2 Human Recombinant produced in E. coli is a single polypeptide chain containing 170 amino acids (22-168) and having a molecular mass of 19kDa. GREM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GREM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
GREM2 which is a member of the BMP (bone morphogenic protein) antagonist family takes part in regulating organogenesis, body patterning, and tissue differentiation. GREM2 is an antagonist of BMP and like BMPs, BMP antagonists contain cystine knots and typically form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, is characterized by a C-terminal cystine knot with an 8-membered ring.
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Synonyms
CKTSF1B2, DAND3, PRDC, Gremlin-2, Cysteine knot superfamily 1, BMP antagonist 2, DAN domain family member 3, Protein related to DAN and cerberus, GREM2.
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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 MGSRKNRPAG AIPSPYKDGS SNNSERWQHQ IKEVLASSQE ALVVTERKYL KSDWCKTQPL RQTVSEEGCR SRTILNRFCY GQCNSFYIPR HVKKEEESFQ SCAFCKPQRV TSVLVELECP GLDPPFRLKK IQKVKQCRCM SVNLSDSDKQ.
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 :
CHGB HumanDescription:
Chromogranin B Human Recombinant
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
Product # :
PRO-824Price :
Quantity :
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Shipped with Ice Packs
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Description
CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
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Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
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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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.
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 :
GCHFR HumanDescription:
GTP Cyclohydrolase I Feedback Regulator Human Recombinant
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
Product # :
PRO-2006Price :
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Description
GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.
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Synonyms
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
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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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.
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 :
Protein-A/G/LDescription:
Protein A/G/L Recombinant
Product # :
PRO-1936Price :
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Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein- A/G/L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.
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 :
CRYAB Human, HisDescription:
Crystallin Alpha B Human Recombinant, His Tag
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-088Price :
Quantity :
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Shipped with Ice Packs
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Description
CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.
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Background
Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.
Structural Insights into CRYAB Human Recombinant:
CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.
Cellular Functions in Proteostasis:
As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.
Implications in Neurodegenerative Disorders:
CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.
CRYAB in Cardiovascular Health:
The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.
Challenges and Future Directions:
While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.
CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.
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 :
SIRT6 HumanDescription:
Sirtuin-6 Human Recombinant
Mono-ADP-ribosyltransferase sirtuin-6, SIR2-like protein 6, SIRT6, SIR2L6, Sirtuin-6.
Product # :
PRO-282Price :
Quantity :
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Shipped with Ice Packs
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Description
SIRT6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (1-355 a.a.) and having a molecular mass of 41 kDa. Recombinant SIRT6 is fused to 20 amino acids His-tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The SIRT6 protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SIRT6 is part of the sirtuin family of proteins (Class IV), homologs to the yeast Sir2 protein. SIRT6 is characterized by a sirtuin core domain. Yeast sirtuin proteins are recognized by their ability to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT6, a chromatin-associated protein is involved in DNA repair. Human Sirtuins function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.
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Synonyms
Mono-ADP-ribosyltransferase sirtuin-6, SIR2-like protein 6, SIRT6, SIR2L6, Sirtuin-6.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL VWQSSSVVFH TGAGISTASG IPDFRGPHGV WTMEERGLAP KFDTTFESAR PTQTHMALVQ LERVGLLRFL VSQNVDGLHV RSGFPRDKLA ELHGNMFVEE CAKCKTQYVR DTVVGTMGLK ATGRLCTVAK ARGLRACRGE LRDTILDWED SLPDRDLALA DEASRNADLS ITLGTSLQIR PSGNLPLATK RRGGRLVIVN LQPTKHDRHA DLRIHGYVDE VMTRLMEHLG LEIPAWDGPR
VLERALPPLP RPPTPKLEPK EESPTRINGS IPAGPKQEPC AQHNGSEPAS PKRERPTSPA PHRPPKRVKA KAVPS.
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 :
CCL28 Human, HisDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28), His Tag
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-366Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCL28 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 126 amino acids (23-127 a.a.) and having a molecular mass of 14.3 kDa. The CCL28 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL28 protein contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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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 MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN, HIS Protein?
CCL28 HUMAN, HIS Protein has a total Mw of 14.3kDa.
What is the source or expression system of CCL28 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN, HIS Protein?
CCL28 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN, HIS Protein?
The biological functionality of CCL28 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL28 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.
What applications can CCL28 HUMAN, HIS Protein be used in?
CCL28 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL28 HUMAN, HIS 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 :
SNCA A30P HumanDescription:
Alpha Synuclein A30P Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-158Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
A-Synuclein A30P Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA A30P protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
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 :
CIDEC HumanDescription:
Cell Death-Inducing DFFA-Like Effector C Human Recombinant
Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.
Product # :
PRO-2026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.
Source
Escherichia Coli.
Formulation
CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.
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Synonyms
Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.
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Physical Appearance
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
MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.
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 :
CTH HumanDescription:
Cystathionase Human Recombinant
Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.
Product # :
ENZ-212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-405) and having a molecular mass of 46.7kDa.CTH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cystathionine gamma-lyase or cystathionase (CTH) is a member of the trans-sulfuration enzymes family. CTH is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate. The CTH catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in the CTH gene cause cystathioninuria.
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Synonyms
Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS.
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 :
TULP1 HumanDescription:
Tubby Like Protein 1 Human Recombinant
Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.
Product # :
PRO-1191Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TULP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 276 amino acids (290-542) and having a molecular mass of 31.1 kDa.TULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TULP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.
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Synonyms
Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.
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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 MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE
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 :
Cyclophilin A MouseDescription:
Cyclophilin A Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
Product # :
ENZ-857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.
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 :
SCRN1 HumanDescription:
Secernin 1 Human Recombinant
Secernin-1, SES1, KIAA0193, Secernin 1.
Product # :
PRO-2212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SCRN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 48.8kDa. SCRN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SCRN1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) , 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.
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Synonyms
Secernin-1, SES1, KIAA0193, Secernin 1.
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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
GSSHHHHHH SSGLVPRGSH MGSMAAAPPS YCFVAFPPRA KDGLVVFGKN SARPRDEVQE VVYFSAADHE PESKVECTYI SIDQVPRTYA IMISRPAWLW GAEMGANEHG VCIANEAINT REPAAEIEAL LGMDLVRLGL ERGETAKEAL DVIVSLLEEH GQGGNYFEDA NSCHSFQSAY LIVDRDEAWV LETIGKYWAA EKVTEGVRCI CSQLSLTTKM DAEHPELRSY AQSQGWWTGE GEFNFSEVFS PVEDHLDCGA GKDSLEKQEE SITVQTMMNT LRDKASGVCI DSEFFLTTAS GVSVLPQNRS SPCIHYFTGT PDPSRSIFKP FIFVDDVKLV PKTQSPCFGD DDPAKKEPRF QEKPDRRHEL YKAHEWARAI IESDQEQGRK LRSTMLELEK QGLEAMEEIL TSSEPLDPAE VGDLFYDCVD TEIKFFK.
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 :
ESAT6-CFP10Description:
ESAT6-CFP10 Chimeric Recombinant
Early Secretory Target Mycobacterium Tuberculosis, ESAT-6
Product # :
PRO-2737Price :
Quantity :
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Description
Recombinant Chimeric ESAT6-CFP10 produced in E. coli is fused to a 6 amino acid his tag at its C-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
ESAT6-CFP10 solution contains 25mM K2CO3, 0.02% NaN3 and PBS.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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Introduction
Mycobacterium antigen ESAT6 has been isolated from low molecular weight fractions of the shot-term-culture filtrate (ST-CF) and it can easily be detected in tuberculosis patients. The export of ESAT-6 which is a potent T-cell antigen, and related proteins requires a dedicated secretory apparatus that is encoded by a group of genes, several of which also code for proteins that are recognized strongly by T cells. The ESAT-6 systems can consequently be considered as immunogenicity islands and there is mounting evidence that the equivalent genes are subject to selective pressure imposed by the immune system of the host. This antigen includes many epitopes detectable in the serum of most patients with tuberculosis (more than 90%). By the attempts to obtain the vaccine on the basis of ESAT-6 it was demonstrated that the optimization of adjuvant is very important when using the combination of dioctadecylammonium bromide and monophosphoryllipide. ESAT-6 is very potential as diagnostic for differentiation between the mycobacterial infection and BCG vaccination. The main topic in ESAT-6 using is in antibody production and in test-systems for tuberculosis elaboration. Early secretory antigen 6 (ESAT6) and cell filtrate protein 10 (CFP10) are 2 antigens secreted as a complex by the replicating Mycobacterium tuberculosis complex (MTC).
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Synonyms
Early Secretory Target Mycobacterium Tuberculosis, ESAT-6
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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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Applications
Immunoassay.
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 :
SDCBP HumanDescription:
Syndecan Binding Protein Human Recombinant
SYCL, syntenin-1, Syndecan-binding protein 1, Scaffold protein Pbp1, MDA-9, Melanoma differentiation-associated protein 9, TACIP18, Pro-TGF-alpha cytoplasmic domain-interacting protein 18.
Product # :
PRO-036Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SDCBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298a.a.) and having a molecular mass of 34.6kDa.SDCBP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SDCBP protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl Buffer (pH 8.0), 100 mM NaCl, and 40% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SDCBP is a multifunctional intracellular adapter protein. SDCBP protein has tandemly repeated PDZ domains which react with the FYA (phe-tyr-ala) carboxyterminal amino acid sequence of the syndecans. SDCBP is has a role in organization of protein complexes in the plasma membranes, regulation of B-cell development, activation of transcription factors, intracellular trafficking and cell-surface targeting, synaptic transmission, and axonal outgrowth.
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Synonyms
SYCL, syntenin-1, Syndecan-binding protein 1, Scaffold protein Pbp1, MDA-9, Melanoma differentiation-associated protein 9, TACIP18, Pro-TGF-alpha cytoplasmic domain-interacting protein 18.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY PELSQYMGLS LNEEEIRANV AVVSGAPLQG QLVARPSSIN YMVAPVTGND VGIRRAEIKQ GIREVILCKD QDGKIGLRLK SIDNGIFVQL VQANSPASLV GLRFGDQVLQ INGENCAGWS SDKAHKVLKQ AFGEKITMTI RDRPFERTIT MHKDSTGHVG FIFKNGKITS IVKDSSAARN GLLTEHNICE INGQNVIGLK
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 :
ZNF689 HumanDescription:
Zinc Finger Protein 689 Human Recombinant
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
Product # :
PRO-1737Price :
Quantity :
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Description
ZNF689 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (1-500a.a) and having a molecular mass of 59.3kDa.ZNF689 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNF689 protein solution (1.0mg/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.
More Info
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Introduction
Zinc Finger Protein 689 (ZNF689) is a member of the krueppel C2H2-type zinc-finger protein family. The ZNF689 protein contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF689 may be involved in transcriptional regulation.
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Synonyms
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
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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 MGSMAPPSAP LPAQGPGKAR PSRKRGRRPR ALKFVDVAVY FSPEEWGCLR PAQRALYRDV MRETYGHLGA LGCAGPKPAL ISWLERNTDD WEPAALDPQE YPRGLTVQRK SRTRKKNGEK EVFPPKEAPR KGKRGRRPSK PRLIPRQTSG GPICPDCGCT FPDHQALESH KCAQNLKKPY PCPDCGRRFS YPSLLVSHRR AHSGECPYVC DQCGKRFSQR KNLSQHQVIH TGEKPYHCPD CGRCFRRSRS LANHRTTHTG EKPHQCPSCG RRFAYPSLLA IHQRTHTGEK PYTCLECNRR FRQRTALVIH QRIHTGEKPY PCPDCERRFS SSSRLVSHRR VHSGERPYAC EHCEARFSQR STLLQHQLLH TGEKPYPCPD CGRAFRRSGS LAIHRSTHTE EKLHACDDCG RRFAYPSLLA SHRRVHSGER PYACDLCSKR FAQWSHLAQH QLLHTGEKPF PCLECGRCFR QRWSLAVHKC SPKAPNCSPR SAIGGSSQRG NAH.
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 :
RPS16 HumanDescription:
Ribosomal Protein S16 Human Recombinant
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
Product # :
PRO-1555Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
RPS16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146) and having a molecular mass of 18.8kDa.RPS16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPS16 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomes are the organelles which catalyze protein synthesis and comprised of a small 40S subunit and a large 60S subunit. Combined, the small 40S and large 60S subunits are composed of 4 RNA types and about 80 structurally distinct proteins. RPS16, a ribosomal protein, is a component of the 40S subunit and a member of the S9P family of ribosomal proteins. RPS16 is situated in the cytoplasm. Just like other genes encoding ribosomal proteins, there are numerous processed pseudogenes of RPS16 spread through the genome.
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Synonyms
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
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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 MGSMPSKGPL QSVQVFGRKK TATAVAHCKR GNGLIKVNGR PLEMIEPRTL QYKLLEPVLL LGKERFAGVD IRVRVKGGGH VAQIYAIRQS ISKALVAYYQ KYVDEASKKE IKDILIQYDR TLLVADPRRC ESKKFGGPGA RARYQKSYR
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 :
SRP19 HumanDescription:
Signal Recognition Particle 19kDa Human Recombinant
Signal recognition particle 19kDa protein, SRP19.
Product # :
PRO-1474Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
SRP19 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 167 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa. The SRP19 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRP19 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Signal recognition particle 19kDa protein (SRP19) is a member of the SRP19 family. SRP19 binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
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Synonyms
Signal recognition particle 19kDa protein, SRP19.
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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 MGSMACAAAR SPADQDRFIC IYPAYLNNKK TIAEGRRIPI SKAVENPTAT EIQDVCSAVG LNVFLEKNKM YSREWNRDVQ YRGRVRVQLK QEDGSLCLVQ FPSRKSVMLY AAEMIPKLKT RTQKTGGADQ SLQQGEGSKK GKGKKKK.
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 :
CENPP HumanDescription:
Centromere Protein-P Human Recombinant
Centromere protein P, CENP-P, CENPP.
Product # :
PRO-1784Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CENPP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-288 a.a) and having a molecular mass of 35.3kDa.CENPP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CENPP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Centromere protein P (CENPP) is component of the CENPA-CAD (nucleosome distal) complex, which is a complex recruited to centromeres and involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENPP protein is involved in incorporation of newly synthesized CENPA into centromeres by way of its interaction with the CENPA-NAC complex.
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Synonyms
Centromere protein P, CENP-P, CENPP.
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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 MDAELAEVRA LQAEIAALRR ACEDPPAPWE EKSRVQKSFQ AIHQFNLEGW KSSKDLKNQL GHLESELSFL STLTGINIRN HSKQTEDLTS TEMTEKSIRK VLQRHRLSGN CHMVTFQLEF QILEIQNKER LSSAVTDLNI IMEPTECSEL SEFVSRAEER KDLFMFFRSL HFFVEWFEYR KRTFKHLKEK YPDAVYLSEG PSSCSMGIRS ASRPGFELVI VWRIQIDEDG KVFPKLDLLT KVPQRALELD KNRAIETAPL SFRTLVGLLG IEAALESLIK SLCAEENN.
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.