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1000 results found for “gliadin”
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Name :
ALCAM (CD166) HumanDescription:
Activated Leukocyte Cell Adhesion Molecule (CD166) Human Recombinant
Activated Leukocyte Cell Adhesion Molecule, CD166 Antigen, MEMD, Activated Leucocyte Cell Adhesion Molecule, CD166, ALCAM.
Product # :
PRO-2388Price :
Quantity :
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Shipped with Ice Packs
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Description
ALCAM Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 742 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa (Molecular size on SDS-PAGE will appear at approximately 70-100 kDa).CD166 is expressed with a 239 amino acid hIgGHis tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD166 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.
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Synonyms
Activated Leukocyte Cell Adhesion Molecule, CD166 Antigen, MEMD, Activated Leucocyte Cell Adhesion Molecule, CD166, ALCAM.
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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
ADPWYTVNSA YGDTIIIPCR LDVPQNLMFG KWKYEKPDGS PVFIAFRSST KKSVQYDDVP EYKDRLNLSE NYTLSISNAR ISDEKRFVCM LVTEDNVFEA PTIVKVFKQP SKPEIVSKAL FLETEQLKKL GDCISEDSYP DGNITWYRNG KVLHPLEGAV VIIFKKEMDP VTQLYTMTST
LEYKTTKADI QMPFTCSVTY YGPSGQKTIH SEQAVFDIYY PTEQVTIQVL PPKNAIKEGD NITLKCLGNG NPPPEEFLFY LPGQPEGIRS SNTYTLTDVR RNATGDYKCS LIDKKSMIAS TAITVHYLDL SLNPSGEVTR QIGDALPVSC TISASRNATV VWMKDNIRLR SSPSFSSLHY
QDAGNYVCET ALQEVEGLKK RESLTLIVEG KPQIKMTKKT DPSGLSKTII CHVEGFPKPA IQWTITGSGS VINQTEESPY INGRYYSKII ISPEENVTLT CTAENQLERT VNSLNVSANE NREKVNDQAK LIVGIVVGLL LAALEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL
MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA
LHNHYTQKSL SLSPGKHHHH HH.
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 :
ANKRD54 HumanDescription:
Ankyrin Repeat Domain 54 Protein Human Recombinant
LIAR, Lyn-interacting ankyrin repeat protein.
Product # :
PRO-1480Price :
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Description
ANKRD54 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a.) and having a molecular mass of 34.9kDa.ANKRD54 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANKRD54 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Ankyrin Repeat Domain 54 (ANKRD54), which is also known as LIAR contains 4 ANK repeats. ANKRD54 plays a vital role in regulating intracellular signaling events related with erythroid terminal differentiation. ANKRD54 interacts with LYN through ankyrin repeat region and the SH3-domain in an activation-independent status of LYN. ANKRD54 creates a multiprotein complex with LYN and HCLS1.
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Synonyms
LIAR, Lyn-interacting ankyrin repeat protein.
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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 MGSMAAAAGD ADDEPRSGHS SSEGECAVAP EPLTDAEGLF SFADFGSALG GGGAGLSGRA SGGAQSPLRY LHVLWQQDAE PRDELRCKIP AGRLRRAARP HRRLGPTGKE VHALKRLRDS ANANDVETVQ QLLEDGADPC AADDKGRTAL HFASCNGNDQ IVQLLLDHGA DPNQRDGLGN TPLHLAACTN HVPVITTLLR GGARVDALDR AGRTPLHLAK SKLNILQEGH AQCLEAVRLE VKQIIHMLRE YLERLGQHEQ RERLDDLCTR LQMTSTKEQV DEVTDLLASF TSLSLQMQSM EKR.
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 :
ARPC2 HumanDescription:
Actin Related Protein 2/3 Complex, Subunit 2 Human Recombinant
ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.
Product # :
PRO-1418Price :
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Shipped with Ice Packs
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Description
ARPC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300a.a) and having a molecular mass of 36.7kDa. ARPC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
ARPC2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Actin-related protein 2/3 complex subunit 2 (ARPC2), is a part of the Rho family of small GTPases and one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. Nevertheless, the exact role of the protein (the p34 subunit) has yet to be determined.
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Synonyms
ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.
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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 MGSMILLEVN NRIIEETLAL KFENAAAGNK PEAVEVTFAD FDGVLYHISN PNGDKTKVMV SISLKFYKEL QAHGADELLK RVYGSFLVNP ESGYNVSLLY DLENLPASKD SIVHQAGMLK RNCFASVFEK YFQFQEEGKE GENRAVIHYR DDETMYVESK KDRVTVVFST VFKDDDDVVI GKVFMQEFKE GRRASHTAPQ VLFSHREPPL ELKDTDAAVG DNIGYITFVL FPRHTNASAR DNTINLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR.
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 :
SPOCK3 MouseDescription:
Sparc/Osteonectin 3 Mouse Recombinant
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
Product # :
PRO-2328Price :
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Shipped with Ice Packs
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Description
SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.
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Synonyms
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
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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
AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH HHH
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 :
BGN Human, Sf9Description:
Biglycan Human Recombinant, Sf9
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
Product # :
PRO-2536Price :
Quantity :
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Description
BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic fibroblast adipose-like cells.
More Info
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Introduction
Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.
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Synonyms
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
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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
ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.
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 :
ITGB1BP3 HumanDescription:
Integrin Beta 1 Binding Protein 3 Human Recombinant
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 2.
Product # :
PRO-1177Price :
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Shipped with Ice Packs
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Description
ITGB1BP3 Human Recombinant produced in E. coli is a single polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 28.4 kDa.ITGB1BP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB1BP3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Nicotinamide riboside kinase 2 (ITGB1BP3) is a member of the uridine kinase family and NRK subfamily. ITGB1BP3 catalyzes the phosphorylation of nicotinic acid riboside and nicotinamide riboside to create nicotinic acid mononucleotide and nicotinamide mononucleotide. ITGB1BP3 reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. ITGB1BP3 is involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. ITGB1BP3 also has a role in the regulation of terminal myogenesis.
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Synonyms
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 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 MGSMKLIVGI GGMTNGGKTT LTNSLLRALP NCCVIHQDDF FKPQDQIAVG EDGFKQWDVL ESLDMEAMLD TVQAWLSSPQ KFARAHGVSV QPEASDTHIL LLEGFLLYSY KPLVDLYSRR YFLTVPYEEC KWRRSTRNYT VPDPPGLFDG HVWPMYQKYR QEMEANGVEV VYLDGMKSRE ELFREVLEDI QNSLLNRSQE SAPSPARPAR TQGPGRGCGH RTARPAASQQ DSM
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 :
ITGB4 HumanDescription:
Integrin Beta 4 Human Recombinant
Integrin beta-4, GP150, CD104, ITGB4, Integrin Subunit Beta 4, CD104 Antigen, Integrin, Beta 4, Integrin Beta-4.
Product # :
PRO-2528Price :
Quantity :
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Shipped with Ice Packs
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Description
ITGB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 691 amino acids (28-710a.a.) and having a molecular mass of 77.5kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ITGB4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ITGB4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ITGB4 (integrin beta-4 isoform 1) belongs to the Integrin beta family. ITGB4 forms noncovalent heterodimers with Integrin alpha 6 and takes part in the formation of epithelial hemidesmosomes. ITGB4 has a vital structural role in the hemidesmosome of epithelial cells and is needed for the regulation of keratinocyte motility & polarity. ITGB4 leans towards the association with alpha 6 subunit and is expected to take a key role in the biology of invasive carcinoma.
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Synonyms
Integrin beta-4, GP150, CD104, ITGB4, Integrin Subunit Beta 4, CD104 Antigen, Integrin, Beta 4, Integrin Beta-4.
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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
NRCKKAPVKS CTECVRVDKD CAYCTDEMFR DRRCNTQAEL LAAGCQRESI VVMESSFQIT EETQIDTTLR RSQMSPQGLR VRLRPGEERH FELEVFEPLE SPVDLYILMD FSNSMSDDLD NLKKMGQNLA RVLSQLTSDY TIGFGKFVDK VSVPQTDMRP EKLKEPWPNS DPPFSFKNVI SLTEDVDEFR NKLQGERISG NLDAPEGGFD AILQTAVCTR DIGWRPDSTH LLVFSTESAF HYEADGANVL AGIMSRNDER CHLDTTGTYT QYRTQDYPSV PTLVRLLAKH NIIPIFAVTN YSYSYYEKLH TYFPVSSLGV LQEDSSNIVE LLEEAFNRIR SNLDIRALDS PRGLRTEVTS KMFQKTRTGS FHIRRGEVGI YQVQLRALEH VDGTHVCQLP EDQKGNIHLK PSFSDGLKMD AGIICDVCTC ELQKEVRSAR CSFNGDFVCG QCVCSEGWSG QTCNCSTGSL SDIQPCLREG EDKPCSGRGE CQCGHCVCYG EGRYEGQFCE YDNFQCPRTS GFLCNDRGRC SMGQCVCEPG WTGPSCDCPL SNATCIDSNG GICNGRGHCE CGRCHCHQQS LYTDTICEIN YSAIHPGLCE DLRSCVQCQA WGTGEKKGRT CEECNFKVKM VDELKRAEEV VVRCSFRDED DDCTYSYTME GDGAPGPNST VLVHKKKDCP PGSLEHHHHH H
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 :
POLD4 HumanDescription:
Polymerase Delta 4 Human Recombinant
DNA polymerase delta subunit 4, p12, POLDS, DNA polymerase delta subunit p12, POLD4, Polymerase Delta 4.
Product # :
PRO-1667Price :
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Shipped with Ice Packs
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Description
POLD4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107) and having a molecular mass of 14.8kDa.POLD4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POLD4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Polymerase Delta 4 also known as POLD4 is the smallest subunit of DNA polymerase delta. DNA polymerase delta which takes a vital part in DNA replication and repair possesses both polymerase and 3' to 5' exonuclease activity. POLD4 increases the activity of DNA polymerase delta and takes a part in fork repair and stabilization during interactions with the DNA helicase Bloom syndrome protein. POLD4 contributes to PCNA-dependent activity of DNA polymerase delta.
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Synonyms
DNA polymerase delta subunit 4, p12, POLDS, DNA polymerase delta subunit p12, POLD4, Polymerase Delta 4.
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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 MGSMGRKRLI TDSYPVVKRR EGPAGHSKGE LAPELGEEPQ PRDEEEAELE LLRQFDLAWQ YGPCTGITRL QRWCRAKQMG LEPPPEVWQV LKTHPGDPRF QCSLWHLYPL.
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 :
PPID MouseDescription:
Peptidylprolyl Isomerase D Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.
Product # :
ENZ-1069Price :
Quantity :
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Shipped with Ice Packs
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Description
PPID Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-370a.a.) and having a molecular mass of 43.4kDa. PPID is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPID protein solution (1mg/ml) containing 20mM Tris-Hcl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700nmol/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-PNA per minute at 37°C in Tris–HCl pH 8.0 using chymotrypsin.
More Info
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Introduction
Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.
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Synonyms
Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.
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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 prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMSHAS PAAKPSNSKN PRVFFDVDIG GERVGRIVLE LFADIVPKTA ENFRALCTGE KGTGSTTGKP LHFKGCPFHR IIKKFMIQGG DFSNQNGTGG ESIYGEKFED ENFHYKHDRE GLLSMANAGP NTNGSQFFIT TVPTPHLDGK HVVFGQVIKG LGVARTLENV EVNGEKPAKL CVIAECGELK EGDDWGIFPK DGSGDSHPDF PEDADIDLKD VDKILLISED LKNIGNTFFK SQNWEMAIKK YAKVLRYVDS SKAVIEKADR SRLQPIALSC VLNIGACKLK MSNWQGAIDS CLEALEMDPS NTKALYRKAQ GWQGLKEYDQ ALADLKKAQE IAPGDKAIQA ELLKVKQMIK AQKDKEKAVY AKMFA.
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 :
GFRA1 RatDescription:
GDNF Family Receptor Alpha 1 Rat Recombinant
GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.
Product # :
CYT-1012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
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Synonyms
GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.
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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
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
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Background
What is the molecular weight/Mw of GFRA1 RAT Protein?
GFRA1 RAT Protein has a total Mw of 72.3kDa.
What is the source or expression system of GFRA1 RAT Protein?
Sf9, Baculovirus cells.
What is the Purity of GFRA1 RAT Protein?
GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GFRA1 RAT Protein?
The biological functionality of GFRA1 RAT Protein will be determined in the future.
What is the amino acid sequence of GFRA1 RAT Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
What applications can GFRA1 RAT Protein be used in?
GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GFRA1 RAT Protein?
The endotoxin level is minimal, GFRA1 RAT 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 :
CDKN2AIPNL HumanDescription:
CDKN2A Interacting Protein N-Terminal Like Human Recombinant
CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.
Product # :
PRO-1865Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDKN2AIPNL Human Recombinant produced in E. coli is. a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.6kDa. CDKN2AIPNL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDKN2AIPNL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
CDKN2A Interacting Protein N-Terminal Like (CDKN2AIPNL) is a part of the CARF family.
-
Synonyms
CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.
-
Physical Appearance
Sterile Filtered clear 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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVGGEAA AAVEELVSGV RQAADFAEQF RSYSESEKQW KARMEFILRH LPDYRDPPDG SGRLDQLLSL SMVWANHLFL GCSYNKDLLD KVMEMADGIE VEDLPQFTTR SELMKKHQS.
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 :
CHCHD7 HumanDescription:
Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7 Human Recombinant
Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7, Coiled-Coil-Helix-Coiled-Coil-Helix Domain-Containing Protein 7, COX23 Cytochrome C Oxidase Assembly Homolog (S. Cerevisiae), COX23 Cytochrome C Oxidase Assembly Homolog , COX23, Coiled-coil-helix-coiled-coil-helix domain-containing protein 7.
Product # :
PRO-2083Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
- purity
- More Info
Description
CHCHD7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97 a.a) and having a molecular mass of 13.9kDa. CHCHD7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CHCHD7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7, also known as CHCHD7 is a newly recognized member of a multifamily of proteins which contains a conserved (coiled coil 1)-(helix 1)-(coiled coil 2)-(helix 2) domain. The biological function of CHCHD7 is unknown and the gene has up till now not been connected with neoplasia. In addition, CHCHD7 & PLAG1 are located head-to-head about 500 bp apart in 8q12. Molecular analyses of twenty seven tumors exposed CHCHD7-PLAG1 fusions in three tumors, two of them had t(6;8) and t(8;15) translocations as a singular anomalies and one a normal karyotype.
-
Synonyms
Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7, Coiled-Coil-Helix-Coiled-Coil-Helix Domain-Containing Protein 7, COX23 Cytochrome C Oxidase Assembly Homolog (S. Cerevisiae), COX23 Cytochrome C Oxidase Assembly Homolog , COX23, Coiled-coil-helix-coiled-coil-helix domain-containing protein 7.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMHQTRTG KKTVRMPSVT QRLRDPDINP CLSESDASTR CLDENNYDRE RCSTYFLRYK NCRRFWNSIV MQRRKNGVKP FMPTAAERDE ILRAVGNMPY.
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 :
LMNA HumanDescription:
Lamin A/C Human Recombinant
Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.
Product # :
PRO-2666Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LMNA Human Recombinant fused with a His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 614 amino acids and having a molecular mass of 68.0kDa. The LMNA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LMNA solution contains 20mM Tris-HCl pH 7.5, 1mM DTT, 0.5M NaCl, 1.5mM EDTA and 20%(v/v) glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. -
Synonyms
Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.
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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
MAHHHHHHVG TGSNDDDDKS PDMETPSQRR ATRSGAQASS TPLSPTRITR LQEKEDLQEL NDRLAVYIDR VRSLETENAG LRLRITESEE VVSREVSGI KAAYEAELGD ARKTLDSVAK ERARLQLELS KVREEFKELK ARNTKKEGDL IAAQARLKDL EALLNSKEAA LSTALSEKRT LEGELHDLRG QVAKLEAALG EAKKQLQDEM LRRVDAENRL QTMKEELDFQ KNIYSEELRE TKRRHETRLV EIDNGKQREF ESRLADALQE LRAQHEDQVE QYKKELEKTY SAKLDNARQS AERNSNLVGA AHEELQQSRI RIDSLSAQLS QLQKQLAAKE AKLRDLEDSL ARERDTSRRL LAEKEREMAE MRARMQQQLD EYQELLDIKL ALDMEIHAYR KLLEGEEERL RLSPSPTSQR SRGRASSHSS QTQGGGSVTK KRKLESTESR SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV TVVEDDEDED GDDLLHHHHG SHCSSSGDPA EYNLRSRTVL CGTCGQPADK ASASGSGAQS PQNCSIM
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 :
MAGEA8 HumanDescription:
Melanoma Antigen Family A, 8 Human Recombinant
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
Product # :
PRO-2206Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAGEA8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 37.6kDa.MAGEA8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAGEA8 protein solution (0.25mg/ml) containing Phosphate Buffered Saline, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Melanoma Antigen Family A 8, also known as MAGEA8 belongs to the MAGE gene family, which includes twelve known genes, of which six are expressed in tumors. Furthermore, the MAGE genes were at first isolated from different kinds of tumors, and according to their virtually exclusive tumor-specific expression in adult tissues, they have been used as targets for cancer immunotherapy.
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Synonyms
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
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Physical Appearance
Sterile Filtered clear 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 MGSMLLGQKS QRYKAEEGLQ AQGEAPGLMD VQIPTAEEQK AASSSSTLIM GTLEEVTDSG SPSPPQSPEG ASSSLTVTDS TLWSQSDEGS SSNEEEGPST SPDPAHLESL FREALDEKVA ELVRFLLRKY QIKEPVTKAE MLESVIKNYK NHFPDIFSKA SECMQVIFGI DVKEVDPAGH SYILVTCLGL SYDGLLGDDQ STPKTGLLII VLGMILMEGS RAPEEAIWEA LSVMGLYDGR EHSVYWKLRK LLTQEWVQEN YLEYRQAPGS DPVRYEFLWG PRALAETSYV KVLEHVVRVN ARVRISYPSL HEEALGEEKG V.
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 :
Exodus-2 Mouse, Sf9Description:
Exodus-2 (CCL21) Mouse Recombinant, Sf9
Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.
Product # :
CHM-043Price :
Quantity :
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Shipped with Ice Packs
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Description
Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.
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Synonyms
Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.
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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
ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH
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 :
CX3CL1 Human, Sf9Description:
Fractalkine (CX3CL1) Human Recombinant, Sf9
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-042Price :
Quantity :
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Shipped with Ice Packs
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- SDS-PAGE
Description
Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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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
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH -
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.
What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.
What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH
What applications can CX3CL1 HUMAN, SF9 Protein be used in?
CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, SF9 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 :
Protein A/GDescription:
Protein A/G Recombinant
Product # :
PRO-646Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The recombinant Protein A/G consists of 5 IgG-binding regions of protein A and 2 of protein G, which corresponds to the Protein A and G domains that are included in the recombinant sequence. Cell wall binding region, cell membrane binding region and albumin binding region have been removed from the recombinant Protein A/G to ensure the maximum specific IgG binding. The Protein A portion is from Staphylococcus aureus segments E, D, A, B and C. The Protein G portion is from Streptococcus segments C1 and C3. The fusion protein has a predicted molecular mass of 47.7kDa and containing 429 amino acids.
Source
Escherichia coli.
Formulation
Lyophilized white Powder containing no additives.
Purity
>97% as determined by SDS-PAGE and RP-HPLC.
More Info
-
Introduction
Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG. -
Stability
After reconstitution, aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Protein-A/G 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 ATKTFTVTE.
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 :
ACVR1 HumanDescription:
Activin A Receptor Type 1 Human Recombinant
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
Product # :
CYT-1140Price :
Quantity :
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- sds-page
Description
ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACVR1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.
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Synonyms
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
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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
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH. -
Background
Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant
1. Abstract
This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.
2. Introduction
The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.
3. Structure and Signaling of ACVR1
ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVR1
Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.
5. ACVR1 in Disease Pathology
The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.
6. Therapeutic Potential of ACVR1
Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.
7. Conclusion and Future Perspectives
While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.
What is the molecular weight / Mw of ACVR1 Protein?
ACVR1 Protein has a total Mw of 38.4kDa.
What is the source or expression system of ACVR1 Protein?
Sf9, Baculovirus cells.
What is the Purity of ACVR1 Protein?
ACVR1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVR1 Protein?
The biological functionality of ACVR1 Protein will be determined in the future.
What is the endotoxin level for ACVR1 Protein?
The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACVR1 Protein?
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
What applications can ACVR1 Protein be used in?
ACVR1 Protein can probably be used in western blot, ELISA and Lateral Flow
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 :
Endostatin HumanDescription:
Endostatin Human Recombinant
Product # :
PRO-248Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
Endostatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide having a predicted molecular mass of 20kDa.C-terminal fragment of collagen XVIII that has been shown to act as a potent inhibitor of angiogenesis and tumor growth in vitro and in vivo. Induces tyrosine phosphorylation of Shc (SH2 domain adapter protein) leading to specific inhibition in endothelial cell proliferation.The Endostatin is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The recombinant Human Endostatin is formulated with 30mM Sodium acetate buffer and Mannitol, pH-5.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity was found to be 16,000IU/mg.More Info
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Introduction
Once a cluster of cancer cells reaches a diameter of about 1–2 mm, it must develop a blood supply in order to grow larger. Given that diffusion is no longer adequate to supply the cancerous cells with oxygen and nutrients and to remove wastes. Therefore, these cells secrete substances that promote the formation of new blood vessels (angiogenesis), which are vital for the growth and persistence of solid tumors and their metastases.
The production of several angiogenic factors (FGF-a, FGF-b, VEGF and VPF) is upregulated by tumors in order to stimulate angiogenesis. However, numerous malignant tumors also generate inhibitors of angiogenesis which include angiostatin and thrombospondin. The angiogenic phenotype is basically the end result of a net balance between the positive and negative regulators of neovascularization mentioned above. Endostatin’s role is to inhibit endothelial proliferation, therefore it is an effective angiogenesis inhibitor. -
Physical Appearance
Sterile filtered liquid formulation.
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Stability
Endostatin should be stored at 2-8°C.Do NOT Freeze!
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 :
OAT AntibodyDescription:
Ornithine aminotransferase, Mouse Anti Human
Ornithine aminotransferase mitochondrial, Ornithine delta-aminotransferase, Ornithine-oxo-acid aminotransferase, OAT, OKT, GACR, HOGA, OATASE, DKFZp781A11155.
Product # :
ANT-013Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
Ornithine aminotransferase is a key enzyme in the pathway that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine aminotransferase (OAT) is a 49kDa nucleus-encoded protein imported into mitochondria to give the mature 48kDa OAT polypeptide. It is found in humans, animals, insects, plants and microorganisms. The OAT has a sex-differential expression in the mouse kidney. OAT plays central physiological roles in amino acid metabolism. OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases that transfer an amino group from a carbon atom which doesn’t carry a carboxyl function. OAT is vital for nitrogen recycling from arginine but not for the stress-induced proline accumulation. OAT enzyme deficiency causes the autosomal recessive eye disease Gyrate Atrophy.
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Synonyms
Ornithine aminotransferase mitochondrial, Ornithine delta-aminotransferase, Ornithine-oxo-acid aminotransferase, OAT, OKT, GACR, HOGA, OATASE, DKFZp781A11155.
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Immunogen
Anti-human OAT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human OAT amino acids 33-439 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Applications
OAT antibody has been tested by by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:250 ~ 500.
Recommended starting dilution is 1:250. -
Type
PAT23A2AT.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
OAT antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
Leptin RatDescription:
Leptin Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-227Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological activity of Leptin Rat is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-His.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a calibrated solution of Leptin rat as a Reference Standard.
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 :
BD 3 RatDescription:
Beta Defensin-3 Rat Recombinant
Beta-defensin 3, BD-3, Defensin beta 3, Defb3.
Product # :
CYT-063Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
BD-3 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.5kDa.The BD-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-3 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.More Info
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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
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Synonyms
Beta-defensin 3, BD-3, Defensin beta 3, Defb3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BD-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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 BD-3 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
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.
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Background
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 4.5kDa.
What is the source or expression system of BD3 Protein?
Escherichia Coli.
What is the Purity of BD3 Protein?
BD3 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD3 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.
What is the amino acid sequence of BD3 Protein?
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.
What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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 :
IL 12 p35 HumanDescription:
Interleukin-12 p35 Human Recombinant
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
Product # :
CYT-487Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
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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.
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 :
IL 16 Human, (130 a.a.)Description:
Interleukin-16 Human Recombinant, (130 a.a.)
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Product # :
CYT-536Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 13.5 kDa. The IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-16 was lyophilized at 1 mg/ml in 10mM NaP, pH-7.5.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis SDS-PAGE.Biological Activity
The ED50 as determined by its ability to chemoattract human CD4+ T lymphocytes using a concentration range of 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.More Info
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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4. -
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL16 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 Interleukin-16 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Asp-Leu-Asn.
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.