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1000 results found for “aprotinin”
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Name :
ARL2 HumanDescription:
ADP-Ribosylation Factor-Like 2 Human Recombinant
ADP-ribosylation factor-like protein 2, ARL2, ARFL2.
Product # :
PRO-074Price :
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Shipped with Ice Packs
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Description
ARL2 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 204 amino acids (1-184 a.a.) and having a molecular mass of 23kDa. The ARL2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 1mM DTT and 40% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ARL2 is a member of the ADP-ribosylation factor (ARF) family. ARL2 functions as a component of a secretory pathway which is involved in the Ca2-dependent release of acetylcholine. ARL2 has a role in the folding of tubule proteins, thus playing a significant role in microtubule dynamics and cell cycle progression. Unlike other members of the ARF family, ARL2 doesn’t act as an activator of the catalytic subunit of cholera toxin.
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Synonyms
ADP-ribosylation factor-like protein 2, ARL2, ARFL2.
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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 MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE ALELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD.
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 :
ARL5B HumanDescription:
ADP-Ribosylation Factor-Like 5B Human Recombinant
ADP-ribosylation factor-like protein 5B, ADP-ribosylation factor-like protein 8, ARL5B, ARL8.
Product # :
PRO-897Price :
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Description
ARL5B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-179 a.a.) and having a molecular mass of 22.5kDa.ARL5B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL5B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol, 0.1M NaCl and 1mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ADP-ribosylation factor-like protein 5B (ARL5B) is a member of a family of proteins which are structurally similar to ADP-ribosylation factors. ARLs and ARFs belong to the RAS superfamily of regulatory GTPases. ARL5B is most closely related to ARL5, with which it shares 80% sequence identity. Furthermore, Human ARL5B shares 100% identity with mouse ARL8 and 71% identity with the Drosophila homolog.
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Synonyms
ADP-ribosylation factor-like protein 5B, ADP-ribosylation factor-like protein 8, ARL5B, ARL8.
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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 MGLIFAKLWS LFCNQEHKVI IVGLDNAGKT TILYQFLMNE VVHTSPTIGS NVEEIVVKNT HFLMWDIGGQ ESLRSSWNTY YSNTEFIILV VDSIDRERLA ITKEELYRML AHEDLRKAAV LIFANKQDMK GCMTAAEISK YLTLSSIKDH PWHIQSCCAL
TGEGLCQGLE WMTSRIGVR.
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 :
ARPP19 HumanDescription:
CAMP-Regulated Phosphoprotein, 19kDa Human Recombinant
CAMP-Regulated Phosphoprotein 19kDa, ARPP-19, ARPP16, Endosulfine Alpha-Like, ARPP-16, ENSAL, CAMP-Regulated Phosphoprotein 19, Cyclic AMP Phosphoprotein 19 KD, ARPP19.
Product # :
PRO-1785Price :
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Description
ARPP19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (1-112 a.a) and having a molecular mass of 14.7kDa.ARPP19 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARPP19 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
cAMP-regulated phosphoprotein 19 (ARPP19) is protein phosphatase inhibitor which specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, ARPP19 specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, a vital condition to maintain cyclin-B1-CDK1 activity high during M phase. ARPP19 protein may indirectly boost GAP-43 expression. The 19 kDa cAMP-regulated phosphoprotein has a role in regulating mitosis by obstructing protein phosphatase-2A.
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Synonyms
CAMP-Regulated Phosphoprotein 19kDa, ARPP-19, ARPP16, Endosulfine Alpha-Like, ARPP-16, ENSAL, CAMP-Regulated Phosphoprotein 19, Cyclic AMP Phosphoprotein 19 KD, ARPP19.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAEVPE AASAEEQKEM EDKVTSPEKA EEAKLKARYP HLGQKPGGSD FLRKRLQKGQ KYFDSGDYNM AKAKMKNKQL PTAAPDKTEV TGDHIPTPQD LPQRKPSLVA SKLAG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ASB13 HumanDescription:
Ankyrin Repeat And SOCS Box Containing 13 Human Recombinant
Ankyrin repeat and SOCS box protein 13, ASB-13, ASB13, ankyrin repeat and SOCS box containing 13.
Product # :
PRO-2060Price :
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Description
ASB13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (1-278 a.a.) and having a molecular mass of 32.4kDa.ASB13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ASB13 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ASB13 belongs to the ankyrin repeat and SOCS box-containing (ASB) family of proteins which contains ankyrin repeat sequence and a SOCS box domain. ASB13 is a protein coding gene that plays a role as a substrate-recognition part of a SCF-like ECS E3 ubiquitin-protein ligase complex which arbitrates the ubiquitination and subsequent proteasomal degradation of target proteins.
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Synonyms
Ankyrin repeat and SOCS box protein 13, ASB-13, ASB13, ankyrin repeat and SOCS box containing 13.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEPRAAD GCFLGDVGFW VERTPVHEAA QRGESLQLQQ LIESGACVNQ VTVDSITPLH AASLQGQARC VQLLLAAGAQ VDARNIDGST PLCDACASGS IECVKLLLSY GAKVNPPLYT ASPLHEACMS GSSECVRLLI DVGANLEAHD CHFGTPLHVA CAREHLDCVK VLLNAGANVN AAKLHETALH HAAKVKNVDL IEMLIEFGGN IYARDNRGKK PSDYTWSSSA PAKCFEYYEK TPLTLSQLCR VNLRKATGVR GLEKIAKLNI PPRLIDYLSY N.
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 :
SPINK1 HumanDescription:
Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
Product # :
ENZ-724Price :
Quantity :
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Shipped with Ice Packs
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Description
SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.
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Synonyms
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
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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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.
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 :
PHB2 HumanDescription:
Prohibitin 2 Human Recombinant
BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.
Product # :
PRO-1533Price :
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Description
PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PHB2 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.
Citations
More Info
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Introduction
Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.
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Synonyms
BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.
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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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.
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 :
CCL4L1 HumanDescription:
LAG-1 Human Recombinant (CCL4L1)
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
Product # :
CHM-018Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa.The CCL4L1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAG-1 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.Citations
More Info
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Introduction
CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.
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Synonyms
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LAG-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4L1 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 LAG-1 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
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.
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Background
What is the molecular weight/Mw of CCL4L1 HUMAN Protein?
CCL4L1 HUMAN Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL4L1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL4L1 HUMAN Protein?
CCL4L1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL4L1 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.
What is the amino acid sequence of CCL4L1 HUMAN Protein?
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.
What applications can CCL4L1 HUMAN Protein be used in?
CCL4L1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL4L1 HUMAN Protein?
The endotoxin level is minimal, CCL4L1 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL4L1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL4L1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VBP1 HumanDescription:
Von Hippel-Lindau Binding Protein 1 Human Recombinant
Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
Product # :
PRO-1325Price :
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Shipped with Ice Packs
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Description
VBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a) and having a molecular mass of 25kDa.VBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VBP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prefoldin subunit 3 (VBP1) is a member of the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein in order to create an intracellular complex. Since VBP1 serves as a chaperone protein, it is assumed to have a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. VBP1 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. VBP1 also binds to nascent polypeptide chain and stimulates folding in an environment in which there are numerous competing pathways for nonnative proteins.
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Synonyms
Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
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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 MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA.
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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Shipped with Ice Packs
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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.
Citations
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 :
ADI1 AntibodyDescription:
Acireductone Dioxygenase 1, Mouse Anti Human
APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.
Product # :
ANT-466Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
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Introduction
Acireductone dioxygenase 1 (ADI1) is a part of the acireductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. ADI1 regulates mRNA processing in the nucleus, and carries out different functions depending on its localization. Related pseudogenes have been defined on chromosomes 8 and 20. ADI1 down-regulates cell migration arbitrated by MMP14.
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Synonyms
APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human ADI1 mAb, clone PAT27E8A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ADI1 protein 1-179 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and Kappa light chain.
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Clone
PAT27E8A.
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Applications
The antibody has been tested by ELISA, Western blot 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 is 1:500 ~ 1:5000. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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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.
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 :
AMELX HumanDescription:
Amelogenin, X-Linked Human Recombinant
Amelogenin X isoform, AMELX, AMG, AMGX, AI1E, AIH1, ALGN, AMGL.
Product # :
PRO-1324Price :
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Shipped with Ice Packs
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Description
AMELX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (17-191 a.a) and having a molecular mass of 22kDa.AMELX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AMELX protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Amelogenin, X-Linked (AMELX) belongs to the amelogenin family of extracellular matrix proteins. Amelogenins have a role biomineralization during tooth enamel development. AMELX gene mutations cause X-linked amelogenesis imperfecta. AMELX regulates the formation of crystallites during the secretory stage of tooth enamel development. AMELX is transiently but amply expressed by ameloblasts during tooth development. Amelogenin is the principal protein in developing dental enamel.
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Synonyms
Amelogenin X isoform, AMELX, AMG, AMGX, AI1E, AIH1, ALGN, AMGL.
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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 MGSMPLPPHP GHPGYINFSY EVLTPLKWYQ SIRPPYPSYG YEPMGGWLHH QIIPVLSQQH PPTHTLQPHH HIPVVPAQQP VIPQQPMMPV PGQHSMTPIQ HHQPNLPPPA QQPYQPQPVQ PQPHQPMQPQ PPVHPMQPLP PQPPLPPMFP MQPLPPMLPD LTLEAWPSTD KTKREEVD.
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 :
NAIF1 HumanDescription:
Nuclear Apoptosis Inducing Factor 1 Human Recombinant
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
Product # :
PRO-1978Price :
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Description
NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
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Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.
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 :
ASB8 HumanDescription:
Ankyrin Repeat And SOCS Box Containing 8 Human Recombinant
Ankyrin Repeat And SOCS Box Containing 8, ASB-8.
Product # :
PRO-1709Price :
Quantity :
Shipping Method :
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Description
ASB8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (1-288) and having a molecular mass of 34.0kDa.ASB8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASB8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ASB8 is a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex that facilitates the ubiquitination and consequent proteasomal degradation of objective proteins.
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Synonyms
Ankyrin Repeat And SOCS Box Containing 8, ASB-8.
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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 MGSMSSSMWY IMQSIQSKYS LSERLIRTIA AIRSFPHDNV EDLIRGGADV NCTHGTLKPL HCACMVSDAD CVELLLEKGA EVNALDGYNR TALHYAAEKD EACVEVLLEY GANPNALDGN RDTPLHWAAF KNNAECVRAL LESGASVNAL DYNNDTPLSW AAMKGNLESV SILLDYGAEV RVINLIGQTP ISRLVALLVR GLGTEKEDSC FELLHRAVGH FELRKNGTMP REVARDPQLC EKLTVLCSAP GTLKTLARYA VRRSLGLQYL PDAVKGLPLP ASLKEYLLLL E
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 :
EFNA5 Human, ActiveDescription:
Ephrin A5 Human Recombinant, Active
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2816Price :
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Description
EFNA5 Human Recombinant is a single, glycosylated, polypeptide chain (21-203 a.a) containing a total of 422 amino acids and having a molecular mass of 48.1 kDa. EFNA5 is fused to a 239 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The EFNA5 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 60 ng/ml measured by its binding ability in a functional ELISA with Mouse EphA3 (CAT# pro-2817).
Citations
More Info
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
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Background
EFNA5 functions through contact-mediated signaling, which can result in either forward signaling (through Eph receptors) or reverse signaling (through ephrins themselves). These signaling pathways regulate various cellular processes such as migration, adhesion, and proliferation. Disruptions or alterations in EFNA5 signaling have been implicated in neurodevelopmental disorders, cancer metastasis, and angiogenesis, highlighting the importance of understanding this protein's roles at a molecular level.
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 :
Streptavidin-NCDescription:
Streptavidin-NC Recombinant
Product # :
PRO-338Price :
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Description
Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.
Source
Escherichia Coli.
Formulation
The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.
Purity
Greater than 93.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Liquid formulation.
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Stability
Streptavidin-NC although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent 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.
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Name :
Trypsin PorcineDescription:
Trypsin Porcine Recombinant
Product # :
PRO-787Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Porcine Trypsin is expressed in E.coli and purified by standard chromatography techniques.
Source
E.coli.
Formulation
The Porcine Trypsin was lyophilized with mannitol as preservative.
Biological Activity
4500 USP units/mg protein.
Citations
More Info
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Introduction
Trypsin (EC3.4.21.4) is part of the serine protease family. Trypsin cleaves lysine and arginine at the C-terminal side of the peptide. The hydrolysis rate is slower if an acidic residue is on either sides of the cleavage site and no cleavage occurs if a proline residue is on the carboxyl side of the cleavage site. Trypsin optimum pH is pH-7 to 9. Trypsin will also hydrolyze ester and amide linkages of synthetic derivatives of amino acids such as: benzoyl L-arginine ethyl ester (BAEE), p-toluenesulfonyl- L-arginine methyl ester (TAME), tosyl-L-arginine methyl ester, N-α-benzoyl-L-arginine p-nitroanilide (BAPNA), L-lysyl-p-nitroanilide, and benzoyl-L-tyrosine ethyl ester (BTEE). Serine protease inhibitors that inhibit recombinant trypsin include TLCK (N-p-tosyl-L-lysine chloromethyl ketone), PMSF (phenylmethanesulfonyl fluoride), benzamidine, soybean trypsin inhibitor, and ovomucoid.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Recombinant Porcine Trypsin although stable at room temp for 1 week, should be stored desiccated 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 Porcine Trypsin in sterile 1mM HCl or 50mM HAC not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNI
DVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCA
AAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGF
LEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWI
QQTIAAN
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Applications
Trypsin digestion: the suggested ratio is 1:50 to 1:1000 (w/w).
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Unit Definition
One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25°C, with BAEE as a substrate (1cm light path).
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 :
Angiostatin K1-4Description:
Angiostatin Kringles 1-4 Human
Product # :
PRO-604Price :
Quantity :
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Description
Human Angiostatin kringles 1-4 is produced from Human Fluid is a glycosylated polypeptide chain which migrates as a doublet 50 kDa on SDS-PAGE. The Ang K1-4 is purified by proprietary chromatographic techniques.
Source
Human Fluid.
Formulation
Lyophilized from a (1mg/ml) solution in containing 20mM Hepes buffer pH-8.2 & 20mM NaCl.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
Human Angiostatin Kringles 1-4 significantly inhibits basic-FGF induced endothelial cell proliferation and migration at concentration ranging from 300nM-1.0 uM.Citations
More Info
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Introduction
There are several proteolytic fragments or specific domains of proteins that act as inhibitors of angiogenesis. These include fragments of plasminogen such as Angiostatin protein kringles 1-4 and kringles 1-5, Endostatin, Restin, PEX, the N-terminal fragment of prolactin, and the Nterminally truncated platelet factor. Angiostatin is a proteolytic protein fragment of plasminogen that is comprised of the first 4 kringle regions. Angiostatin k1-4 prevents the growth of endothelial cells, and its systemic administration inhibits the growth of primary carcinomas in mice. Angiostatin Kringles 1-3 segment has a larger inhibitory activity than the Angiostatin kringles 1-4 fragment. The protease-activated angiostatin kringles 1-5 is the most potent plasminogen fragment with over 50 times larger endothelial cell specific inhibitory activity. Angiostatin kringles 1-5 systemic administration inhibits growth of fibrosarcoma and significantly reduces neovascularization.
Angiostatin is an angiogenesis inhibitor in mouse serum and urine. Angiostatin is a 38 kDa protein fragment of the plasminogen composed of the 1st 4 kringle domains of plasminogen. Angiostatin K1-4 is also named plasminogen kringles 1-4 and PK1-4.
Angiostatin protein is manufactured by the protelytic cleavage of plasminogen by a serine protease from several prostate carcinoma cell lines. The manufacturing of angiostatin by pancreatic cancer cells can be inhibited by TGF-beta 1 along with plasminogen activator inhibitor type-1 (PAI1). -
Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized Angiostatin Kringles 1-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Angiostatin Kringles1-4 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 Angiostatin K1-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
FABP4 ProteinDescription:
Fatty Acid Binding Protein 4 Human Recombinant
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
Product # :
PRO-416Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
14.7kDa protein containing 132 amino acid residues.
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH4.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages. -
Synonyms
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM KGVTSTRVYE RA.
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Specificity
The amino acid sequence of the recombinant human FABP4 is 100% homologous to the amino acid sequence of the human FABP4.
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Purification Method
Two-step procedure using size exclusion chromatography before and after refolding.
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 :
Aln G 4.0101Description:
Polcalcin Aln g 4 Recombinant
Polcalcin Aln g 4, Calcium-binding pollen allergen Aln g 4, Aln g 4.
Product # :
PRO-2281Price :
Quantity :
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Description
Recombinant Polcalcin Aln g 4 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 10,185 Dalton. Aln G 4.0101 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Aln G 4.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Polcalcin Aln g 4 (Aln G 4.0101) causes an allergic reaction in humans.
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Synonyms
Polcalcin Aln g 4, Calcium-binding pollen allergen Aln g 4, Aln g 4.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
Streptolysin-ODescription:
Streptolysin-O Streptococcus Pyogenes Recombinant
Streptolysin O, Thiol-activated cytolysin, slo.
Product # :
PRO-2302Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.The Streptolysin-O is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Streptolysin-O protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.
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Synonyms
Streptolysin O, Thiol-activated cytolysin, slo.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Streptolysin-O although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptolysin-O 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 Streptolysin-O 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
NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.
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 :
GAL HumanDescription:
Galanin Prepropeptide Human Recombinant
GALN, GLNN, GMAP, GAL, GAL1.
Product # :
PRO-1433Price :
Quantity :
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Description
GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.
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Synonyms
GALN, GLNN, GMAP, GAL, GAL1.
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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 MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.
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 :
ANPEP MouseDescription:
Alanyl Aminopeptidase Membrane Mouse Recombinant
Anpep, AP-M, AP-N, Apn, Cd13, P150, mAPN, Alanyl aminopeptidase, Aminopeptidase M, Membrane protein p161, Microsomal aminopeptidase, CD13, Lap-1, Lap1, aminopeptidase N.
Product # :
ENZ-1134Price :
Quantity :
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Description
ANPEP Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 943 amino acids (33-966 a.a.) and having a molecular mass of 107.5 kDa. ANPEPis expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ANPEP protein solution ( 0.5mg/ml ) contains PBS (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 4,000pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of H-AlaAMC to Alanine and AMC per minute at pH7.5 at 25C.
Citations
More Info
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Introduction
ANPEP or aminopeptidase N, is an enzyme, found in the small-intestinal and renal microvillar membrane and other plasma membranes. The enzyme has a critical part in the digestion of peptides after their hydrolysis by gastric and pancreatic proteases. ANPEP is also part ofthe processing of different peptides as well as peptide hormones, neuropeptides & chemokines. The protein takes part in angiogenesis, enhancing cholesterol crystallization &amino acid transport by formatting with SLC6A19 transport protein and regulating its activity.
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Synonyms
Anpep, AP-M, AP-N, Apn, Cd13, P150, mAPN, Alanyl aminopeptidase, Aminopeptidase M, Membrane protein p161, Microsomal aminopeptidase, CD13, Lap-1, Lap1, aminopeptidase N.
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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
ADPYAQEKNR NAENSATAPT LPGSTSATTA TTTPAVDESK PWNQYRLPKT LIPDSYRVIL RPYLTPNNQG LYIFQGNSTV RFTCNQTTDV IIIHSKKLNY TLKGNHRVVL RTLDGTPAPN IDKTELVERT EYLVVHLQGS LVEGRQYEMD SQFQGELADD LAGFYRSEYM EGDVKKVVAT TQMQAADARK SFPCFDEPAM KAMFNITLIY PNNLIALSNM LPKESKPYPE DPSCTMTEFH STPKMSTYLL AYIVSEFKNI SSVSANGVQI GIWARPSAID EGQGDYALNV TGPILNFFAQ HYNTSYPLPK SDQIALPDFN AGAMENWGLV TYRESSLVFD SQSSSISNKE RVVTVIAHEL AHQWFGNLVT VAWWNDLWLN EGFASYVEYL GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSSPAD EIKTPDQIME LFDSITYSKG ASVIRMLSSF LTEDLFKKGL SSYLHTYQYS NTVYLDLWEH LQKAVNQQTA VQPPATVRTI MDRWILQMGF PVITVNTNTG EISQKHFLLD SKSNVTRPSE FNYIWIAPIP FLKSGQEDHY WLDVEKNQSA KFQTSSNEWI LLNINVTGYY LVNYDENNWK KLQNQLQTDL SVIPVINRAQ IIHDSFNLAS AKMIPITLAL DNTLFLVKEA EYMPWQAALS SLNYFTLMFD RSEVYGPMKR YLKKQVTPLF FYFQNRTNNW VNRPPTLMEQ YNEINAISTA CSSGLKECRD LVVELYSQWM KNPNNNTIHP NLRSTVYCNA IAFGGEEEWN FAWEQFRNAT LVNEADKLRS ALACSKDVWI LNRYLSYTLN PDYIRKQDTT STIISIASNV AGHPLVWDFV RSNWKKLFEN YGGGSFSFAN LIQGVTRRFS SEFELQQLEQ FKADNSATGF GTGTRALEQA LEKTRANIDW VKENKDAVFK WFTENSSHHH 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.
- View Data Sheet
Name :
OmpADescription:
Outer Membrane Protein-A Bacterial Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-571Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.Citations
More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.
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 :
BNP ProteinDescription:
B-type Natriuretic Peptide Human Recombinant
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NPPB 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 B-type Natriuretic Peptide 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
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
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Background
What is the molecular weight / Mw of BNP Protein?
BNP Protein has a total Mw of 3.5kDa.
What is the source or expression system of BNP Protein?
Escherichia Coli.
What is the Purity of BNP Protein?
BNP Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP Protein?
The biological functionality of BNP Protein will be determined in the future.
What is the amino acid sequence of BNP Protein?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
What applications can BNP Protein Protein be used in?
BNP Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP Protein?
The endotoxin level is minimal, BNP 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.