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1000 results found for “Proteasome”
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Name :
PPP1R3B HumanDescription:
Protein Phosphatase 1, Regulatory Subunit 3B Human Recombinant
Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.
Product # :
PRO-1700Price :
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Description
PPP1R3B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285) and having a molecular mass of 35.1 kDa.PPP1R3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPP1R3B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein Phosphatase 1, Regulatory Subunit 3B (PPP1R3B) is the catalytic subunit of the serine/theonine phosphatase, protein phosphatase-1. PPP1R3B, which is expressed both in liver and in skeletal muscle tissue, regulates glycogen synthesis in these tissues. PPP1R3B is involved in type 2 diabetes and maturity-onset diabetes of the young.
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Synonyms
Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.
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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 MGSMMAVDIE YRYNCMAPSL RQERFAFKIS PKPSKPLRPC IQLSSKNEAS GMVAPAVQEK KVKKRVSFAD NQGLALTMVK VFSEFDDPLD MPFNITELLD NIVSLTTAES ESFVLDFSQP SADYLDFRNR LQADHVCLEN CVLKDKAIAG TVKVQNLAFE KTVKIRMTFD TWKSYTDFPC QYVKDTYAGS DRDTFSFDIS LPEKIQSYER MEFAVYYECN GQTYWDSNRG KNYRIIRAEL KSTQGMTKPH SGPDLGISFD QFGSPRCSYG LFPEWPSYLG YEKLGPYY.
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 :
CHRAC1 HumanDescription:
Chromatin Accessibility Complex 1 Human Recombinant
CHARC1, CHARC15, CHRAC-1, CHRAC-15, CHRAC15, YCL1, Chromatin accessibility complex protein 1, Chromatin accessibility complex 15 kDa protein, DNA polymerase epsilon subunit p15.
Product # :
PRO-1391Price :
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Description
CHRAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131 a.a.) and having a molecular mass of 17.1kDa. CHRAC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CHRAC1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Chromatin Accessibility Complex 1 (CHRAC1) is a histone-fold protein which interacts with further histone-fold proteins to bind DNA in a sequence-independent mode. These histone-fold protein dimers combine within larger enzymatic complexes for DNA replication, transcription, and packaging.
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Synonyms
CHARC1, CHARC15, CHRAC-1, CHRAC-15, CHRAC15, YCL1, Chromatin accessibility complex protein 1, Chromatin accessibility complex 15 kDa protein, DNA polymerase epsilon subunit p15.
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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 MGSMADVVVG KDKGGEQRLI SLPLSRIRVI MKSSPEVSSI NQEALVLTAK ATELFVQCLA TYSYRHGSGK EKKVLTYSDL ANTAQQSETF QFLADILPKK ILASKYLKML KEEKREEDEE NDNDNESDHD EADS.
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 :
RPL11 HumanDescription:
Ribosomal Protein L11 Human Recombinant
Ribosomal Protein L11, Cell Growth-Inhibiting Protein 34, CLL-Associated Antigen KW-12, 60S Ribosomal Protein L11, DBA7, GIG34, L11.
Product # :
PRO-1561Price :
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Description
RPL11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 22.6kDa.RPL11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPL11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT, 2mM EDTA, 250mM Imidazole and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomes are the organelles which catalyze protein synthesis, they’re comprised of a small 40S subunit and a large 60S subunit. Ribosomal Protein L11 (RPL11) is a member of the L5P family of ribosomal proteins. RPL11 is a ribosomal protein which is a component of the 60S subunit. RPL11 is found in the cytoplasm. The RPL11 protein most likely associates with the 5S rRNA.
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Synonyms
Ribosomal Protein L11, Cell Growth-Inhibiting Protein 34, CLL-Associated Antigen KW-12, 60S Ribosomal Protein L11, DBA7, GIG34, L11.
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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 MGSMAQDQGE KENPMRELRI RKLCLNICVG ESGDRLTRAA KVLEQLTGQT PVFSKARYTV RSFGIRRNEK IAVHCTVRGA KAEEILEKGL KVREYELRKN NFSDTGNFGF GIQEHIDLGI KYDPSIGIYG LDFYVVLGRP GFSIADKKRR TGCIGAKHRI SKEEAMRWFQ QKYDGIILPG K
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 :
CTSD MouseDescription:
Cathepsin-D Mouse Recombinant
Ctsd, CatD, CD, Cathepsin D.
Product # :
ENZ-1017Price :
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Description
CTSD produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-410 a.a.) and having a molecular mass of 44.0kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSD is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSD 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.
Biological Activity
Specific activity is > 1,000 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.More Info
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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
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Synonyms
Ctsd, CatD, CD, Cathepsin 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). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
IIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS PKTTEPVSEL LKNYLDAQYY GDIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KILDIACWVH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDQSKARGI KVEKQIFGEA TKQPGIVFVA AKFDGILGMG YPHISVNNVL PVFDNLMQQK LVDKNIFSFY LNRDPEGQPG GELMLGGTDS KYYHGELSYL NVTRKAYWQV HMDQLEVGNE LTLCKGGCEA IVDTGTSLLV GPVEEVKELQ KAIGAVPLIQ GEYMIPCEKV SSLPTVYLKL GGKNYELHPD KYILKVSQGG KTICLSGFMG MDIPPPSGPL WILGDVFIGS YYTVFDRDNN RVGFANAVVL LEHHHHHH.
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 :
F7 HumanDescription:
Coagulation Factor VIIa Human Recombinant
Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.
Product # :
PRO-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Factor VIIa Human Recombinant produced in BHK is a glycosylated polypeptide two-chain dimer consisting of 406 amino acids with a molecular weight of 50kD.The Factor-VIIa is purified by proprietary chromatographic techniques.
Source
BHK cells (Baby Hamster Kidney Cells).
Formulation
The protein 1 mg/ml was lyophilized after from a sterile solution containing 10mg sucrose pH-6.
Purity
Greater than 98.0% as determined by analysis by SDS-PAGE.
Biological Activity
The potency per mg was tested and found to be 50,000Units/mg.More Info
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Introduction
Coagulation factor VII is a vitamin K-dependent factor which is essential for hemostasis. It circulates in the blood as a zymogen which is later converted to an active form by factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of factor VII, a heavy chain with a catalytic domain and a light chain with 2 EGF-like domains are generated, and the two chains are held together by a disulfide bond. The presence of factor III and calcium ions further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Alternative splicing of factor VII results in 2 transcripts. Defects in coagulation factor VII can cause coagulopathy. Coagulation factor VII initiates the extrinsic pathway of blood coagulation. Minor proteolysis converts factor VII to factor VIIa by factors Xa, XIIa, IXa, or thrombin. Factor VIIa also converts factor IX to factor IXa in the presence of tissue factor and calcium.
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Synonyms
Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Factor-VIIa although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIIa 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 Factor-VIIa 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 :
Apolipoprotein A1 Human, HisDescription:
Apolipoprotein A-I Human Recombinant, His Tag
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Product # :
CYT-661Price :
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- sds-page
Description
APOA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (25-267 a.a.) and having a molecular mass of 30.3kDa. APOA1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The APOA1 solution containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
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Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
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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 MDEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
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Background
What is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein has a total Mw of 30.3kDa.
What is the source or expression system of APOLIPOPROTEIN A1 Protein?
Escherichia Coli.
What is the Purity of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.
What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
MGSSHHHHHH SSGLVPRGSH MDEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ
What applications can APOLIPOPROTEIN A1 Protein be used in?
APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
The endotoxin level is minimal, APOLIPOPROTEIN A1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C4c HumanDescription:
Complement Component C4c Human
Complement C4c, Complement Component C4c, C4c.
Product # :
PRO-556Price :
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Description
Human C4c produced in Human plasma having a molecular mass of 210 kDa.
Source
Human Plasma.
Formulation
The Human Complement C4c solution is in Sodium Phosphate buffer pH 7.0 containing 0.15M NaCl and 0.09% NaN3.
Purity
Greater than 99.0%.
More Info
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Introduction
Complement C4c is a degradation product of C4b which is cleaved by C4b/C3b inactivator to yield C4d and C4c.
Complement C4c interacts with C1 and C2 to form C3 convertase of the classic activation pathway. Systemic lupus erythematosus (SLE) is often associated with congenital C4 deficiency. Reduced levels of components of the classic pathway (C1, C2, C4, C3) are common after such activation, e.g. in SLE, acute serum sickness and conditions associated with circulating immune complexes. -
Synonyms
Complement C4c, Complement Component C4c, C4c.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Human C4c although stable at 4°C for 1 week, should be stored at -15°C.Please avoid freeze-thaw cycles.
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Human Virus Test
Plasma from each donor has been tested and found negative for HIV-1 & 2 antibodies, Hepatatis B surface antigen, and Hepatatis C antibodies.
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 :
ARF4 HumanDescription:
ADP-Ribosylation Factor 4 Human Recombinant
ADP-ribosylation factor 4, ARF4, ARF2.
Product # :
PRO-066Price :
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Shipped with Ice Packs
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Description
ARF4 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 204 amino acids (1-180 a.a.) and having a molecular mass of 23kDa. The ARF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF4 solution (0.5 mg/ml) in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ARF4 belongs to the ARF gene family whose members encode small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. The ARF proteins include five ARF proteins and eleven ARF-like proteins and constitute one family of the RAS superfamily. They are classified as class I, class II and class III; the ARF4 gene is a class II member. The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains 6 exons and 5 introns. The ARF4 gene is the most divergent member of the human ARFs.
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Synonyms
ADP-ribosylation factor 4, ARF4, ARF2.
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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 MGSHMGLTIS SLFSRLFGKK QMRILMVGLD AAGKTTILYK LKLGEIVTTI PTIGFNVETV EYKNICFTVW DVGGQDRIRP LWKHYFQNTQ GLIFVVDSND RERIQEVADE LQKMLLVDEL RDAVLLLFAN KQDLPNAMAI SEMTDKLGLQ SLRNRTWYVQ ATCATQGTGL YEGLDWLSNE LSKR.
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 :
COMMD7 HumanDescription:
COMM Domain Containing 7 Human Recombinant
C20orf92, dJ1085F17.3.
Product # :
PRO-1481Price :
Quantity :
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Description
COMMD7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200 a.a.) and having a molecular mass of 24.9kDa.COMMD7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COMMD7 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
COMM Domain Containing 7 (COMMD7) composed of 200 amino acid which contains 1 COMM domain. COMMD7 interacts (through COMM domain) with COMMD1 via its COMM domain.COMMD7 also associates with the NF-kappa-B complex and suppresses its transcriptional activity. COMMD7 is highly expressed in lung.
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Synonyms
C20orf92, dJ1085F17.3.
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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 MGSMGRLHCT EDPVPEAVGG DMQQLNQLGA QQFSALTEVL FHFLTEPKEV ERFLAQLSEF ATTNQISLGS LRSIVKSLLL VPNGALKKSL TAKQVQADFI TLGLSEEKAT YFSEKWKQNA PTLARWAIGQ TLMINQLIDM EWKFGVTSGS SELEKVGSIF LQLKLVVKKG NQTENVYIEL TLPQFYSFLH EMERVRTSME CFC.
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 :
FAP HumanDescription:
Fibroblast Activation Protein Alpha Human Recombinant
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP
Product # :
ENZ-1160Price :
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Shipped with Ice Packs
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Description
FAP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 744 amino acids (26-760aa) and having a molecular mass of 86.1 kDa.FAP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FAP solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 5,000 pmol/min/ug. It is defined by the amount of enzyme that hydrolyzes 1.0 pmole of ZGP-AMC per minute at pH 7.5, at 37˚C.
More Info
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Introduction
DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.
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Synonyms
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP
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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
ADPLRPSRVH NSEENTMRAL TLKDILNGTF SYKTFFPNWI SGQEYLHQSA DNNIVLYNIE TGQSYTILSN RTMKSVNASN YGLSPDRQFV YLESDYSKLW RYSYTATYYI YDLSNGEFVR GNELPRPIQY LCWSPVGSKL AYVYQNNIYL KQRPGDPPFQ ITFNGRENKI FNGIPDWVYE EEMLATKYAL WWSPNGKFLA YAEFNDTDIP VIAYSYYGDE QYPRTINIPY PKAGAKNPVV RIFIIDTTYP AYVGPQEVPV PAMIASSDYY FSWLTWVTDE RVCLQWLKRV QNVSVLSICD FREDWQTWDC PKTQEHIEES RTGWAGGFFV STPVFSYDAI SYYKIFSDKD GYKHIHYIKD TVENAIQITS GKWEAINIFR VTQDSLFYSS NEFEEYPGRR NIYRISIGSY PPSKKCVTCH LRKERCQYYT ASFSDYAKYY ALVCYGPGIP ISTLHDGRTD QEIKILEENK ELENALKNIQ LPKEEIKKLE VDEITLWYKM ILPPQFDRSK KYPLLIQVYG GPCSQSVRSV FAVNWISYLA SKEGMVIALV DGRGTAFQGD KLLYAVYRKL GVYEVEDQIT AVRKFIEMGF IDEKRIAIWG WSYGGYVSSL ALASGTGLFK CGIAVAPVSS WEYYASVYTE RFMGLPTKDD NLEHYKNSTV MARAEYFRNV DYLLIHGTAD DNVHFQNSAQ IAKALVNAQV DFQAMWYSDQ NHGLSGLSTN HLYTHMTHFL KQCFSLSDHH HHHH
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 :
PTPN11 HumanDescription:
Protein Tyrosine Phosphatase Non Receptor Type-11 Human Recombinant
Protein Tyrosine Phosphatase, Non-Receptor Type 11, Protein-Tyrosine Phosphatase 1D, Protein-Tyrosine Phosphatase 2C, EC 3.1.3.48, SH-PTP2, SH-PTP3, PTP-1D, PTP-2C, PTP2C, SHP2, Tyrosine-Protein Phosphatase Non-Receptor Type 11, Noonan Syndrome 1, METCDS, SHPTP2, BPTP3, SHP-2, JMML, NS1, CFC, PTPN11.
Product # :
PKA-109Price :
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Description
PTPN11 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 469 amino acids (1-460a.a.) and having a molecular mass of 53.9kDa. PTPN11 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PTPN11 protein 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
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Introduction
Astyrosine-protein phosphatase non-receptor type 11 isoform 2 (PTPN11), is a member of the protein-tyrosine phosphatase family, non-receptor class 2 subfamily. PTPN11 takes part in signal transduction from the cell surface to the nucleus downstream of various cytosolic protein tyrosine kinases as well as receptors. PTPN11 deficient cells have poor mobility due to excessive phosphorylation of FAK as well as other proteins which interfere with the rotation of cell attachment points in the focal adhesion complex.
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Synonyms
Protein Tyrosine Phosphatase, Non-Receptor Type 11, Protein-Tyrosine Phosphatase 1D, Protein-Tyrosine Phosphatase 2C, EC 3.1.3.48, SH-PTP2, SH-PTP3, PTP-1D, PTP-2C, PTP2C, SHP2, Tyrosine-Protein Phosphatase Non-Receptor Type 11, Noonan Syndrome 1, METCDS, SHPTP2, BPTP3, SHP-2, JMML, NS1, CFC, PTPN11.
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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
ADPMTSRRWF HPNITGVEAE NLLLTRGVDG SFLARPSKSN PGDFTLSVRR NGAVTHIKIQ NTGDYYDLYG GEKFATLAEL VQYYMEHHGQ LKEKNGDVIE LKYPLNCADP TSERWFHGHL SGKEAEKLLT EKGKHGSFLV RESQSHPGDF VLSVRTGDDK GESNDGKSKV THVMIRCQEL KYDVGGGERF DSLTDLVEHY KKNPMVETLG TVLQLKQPLN TTRINAAEIE SRVRELSKLA ETTDKVKQGF WEEFETLQQQ ECKLLYSRKE GQRQENKNKN RYKNILPFDH TRVVLHDGDP NEPVSDYINA NIIMPEFETK CNNSKPKKSY IATQGCLQNT VNDFWRMVFQ ENSRVIVMTT KEVERGKSKC VKYWPDEYAL KEYGVMRVRN VKESAAHDYT LRELKLSKVG QGNTERTVWQ YHFRTWPDHG VPSDPGGVLD FLEEVHHKQE SIMDAGPVVV HCRHHHHHH
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 :
Apolipoprotein A1 HumanDescription:
Apolipoprotein A-I Human Recombinant
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Product # :
CYT-750Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Apolipoprotein A-I Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids and having a molecular mass of 28.1kDa.The APOA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The APOA1 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.More Info
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Introduction
APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
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Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Apolipoprotein A-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOA1 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 APOA1 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
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
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Background
Apolipoprotein A-I Human Recombinant: A Promising Therapeutic Agent for Cardiovascular Diseases
Abstract:
Cardiovascular diseases (CVDs) remain a leading cause of mortality worldwide. Dyslipidemia, characterized by abnormal lipid profiles, is a significant risk factor for the development of CVDs. Apolipoprotein A-I (ApoA-I) is the primary protein component of high-density lipoprotein (HDL), known as the "good cholesterol." ApoA-I plays a crucial role in reverse cholesterol transport, promoting the efflux of cholesterol from peripheral tissues to the liver for elimination. Recombinant ApoA-I offers a potential therapeutic strategy for enhancing HDL functionality and reducing CVD risk. This research paper aims to provide an overview of ApoA-I human recombinant, its production methods, and its therapeutic applications in cardiovascular medicine.Introduction
Cardiovascular diseases and dyslipidemia
Role of apolipoprotein A-I in reverse cholesterol transport
Potential of ApoA-I human recombinant as a therapeutic agentStructure and Function of Apolipoprotein A-I
Primary structure and domains of ApoA-I
Functional properties of ApoA-I in reverse cholesterol transport
Interaction with other lipoproteins and cellular receptorsProduction of Apolipoprotein A-I Human Recombinant
Expression systems for recombinant ApoA-I
Biotechnological methods for large-scale production
Purification and characterization of recombinant ApoA-ITherapeutic Applications of Apolipoprotein A-I Human Recombinant
Promotion of reverse cholesterol transport
Anti-inflammatory and antioxidant effects
Enhancement of endothelial function
Cardioprotective effects in animal modelsClinical Trials and Future Perspectives
Phase I and II clinical trials
Challenges and limitations
Future directions and potential therapeutic combinationsConclusion
Summary of the potential of ApoA-I human recombinant as a therapeutic agent for CVDs
Importance of ongoing research and clinical trialsWhat is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein has a total Mw of 28.1kDa.
What is the source or expression system of APOLIPOPROTEIN A1 Protein?
Escherichia Coli.
What is the Purity of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.
What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
What applications can APOLIPOPROTEIN A1 Protein be used in?
APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
The endotoxin level is minimal, APOLIPOPROTEIN A1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Histone BovineDescription:
Bovine Histone
Product # :
PRO-2558Price :
Quantity :
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Description
Histone Bovine is purified from bovine tissues by proprietary protein-chemical techniques.
Source
Bovine tissues.
Formulation
Histone Bovine is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Histone is vastly alkaline protein exists in eukaryotic cell nuclei which set and direct the DNA into structural units named nucleosomes. 5 key families of histones are: H1/H5, H2A, H2B, H3, including H4. The core histones are H2A, H2B, H3 and H4, whereas histones H1/H5 are identified as the linker histones. Moreover the dynamics of chromatin structure depend on posttranslational modification of histones in addition to the appearance of different histone variants. Histone H3 as well as H4 are modified covalently at several residues. The histone code is constitute by these and the H2A/H2B modifications.
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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 IgG type human auto antibodies.2. Checkerboard/immunodot analysis of positive/negative samples.
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coating concentration
0.2-0.5 μg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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 :
Desmin ChickenDescription:
Desmin Chicken Gizzard
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-2783Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.
Source
Chicken gizzard.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.
The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.
The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.
The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.
By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.
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 :
SIL1 HumanDescription:
SIL1 Human Recombinant
SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.
Product # :
PRO-1187Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 439 amino acids (32-461) and having a molecular mass of 50.0 kDa.SIL1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SIL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SIL1 is localized to endoplasmic reticulum (ER). SIL1 is an N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. SIL1 acts as a nucleotide exchange factor for another unfolded protein response protein. Mutations in SIL1 are linked to Marinesco-Sjogren syndrome.
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Synonyms
SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.
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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
MHQNLKEFAL TNPEKSSTKE TERKETKAEE ELDAEVLEVF HPTHEWQALQ PGQAVPAGSH VRLNLQTGER EAKLQYEDKF RNNLKGKRLD INTNTYTSQD LKSALAKFKE GAEMESSKED KARQAEVKRL FRPIEELKKD FDELNVVIET DMQIMVRLIN KFNSSSSSLE EKIAALFDLE YYVHQMDNAQ DLLSFGGLQV VINGLNSTEP LVKEYAAFVL GAAFSSNPKV QVEAIEGGAL QKLLVILATE QPLTAKKKVL FALCSLLRHF PYAQRQFLKL GGLQVLRTLV QEKGTEVLAV RVVTLLYDLV TEKMFAEEEA ELTQEMSPEK LQQYRQVHLL PGLWEQGWCE ITAHLLALPE HDAREKVLQT LGVLLTTCRD RYRQDPQLGR TLASLQAEYQ VLASLELQDG EDEGYFQELL GSVNSLLKEL RLEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Protein-A/G/L-CysDescription:
Protein A/G/L-Cys Recombinant
Product # :
PRO-1934Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein- A/G/L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.
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 HumanDescription:
Biglycan Human Recombinant
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
Product # :
PRO-1382Price :
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Shipped with Ice Packs
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Description
BGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (38-368a.a) and having a molecular mass of 39.5kDa. BGN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
BGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
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
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
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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 MDEEASGADT SGVLDPDSVT PTYSAMCPFG CHCHLRVVQC SDLGLKSVPK EISPDTTLLD LQNNDISELR KDDFKGLQHL YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK GVFSGLRNMN CIEMGGNPLE NSGFEPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLARVPSGL PDLKLLQVVY LHSNNITKVG VNDFCPMGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT DRLAIQFGNY 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 :
FIS1 HumanDescription:
Fission-1 Human Recombinant
TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).
Product # :
PRO-829Price :
Quantity :
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Shipped with Ice Packs
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Description
FIS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids (1-122 a.a.) and having a molecular mass of 16.3 kDa. FIS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
FIS1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 induces cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. FIS1 participates in peroxisomal growth and division. The C terminus is required for mitochondrial localisation, while the N teminus is necessary for mitochondrial fission.
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Synonyms
TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).
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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 MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK DG.
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 :
LIN28 Human, TATDescription:
LIN28-TAT Human Recombinant
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
Product # :
PRO-2495Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (including 13- residue C-terminal TAT peptide) and having a molecular mass of 24.4kDa. The LIN28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LIN28 protein solution was formulated in PBS with 50mM arginine
Purity
Greater than 90% as determined by SDS-PAGE (coomassie staining).
More Info
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Introduction
LIN28 is a marker of undifferentiated human embryonic stem cells and it increases the productivity of the formation of induced pluripotent stem cells from human fibroblasts. LIN28 acts as a 'translational enhancer and therefore leading specific mRNAs to polysomes and causes an increased protein synthesis. LIN28 binds let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells.
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Synonyms
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
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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
GPSVSNQQFA GGCAKAAEEA PEEAPEDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS ERRPKGKSMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSISHM VASCPLKAQQ GPSAQGKPTY FREEEEEIHS PTLLPEAQNG GYGRKKRRQR RR.
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 :
Lamin-A HumanDescription:
Lamin-A Human Recombinant
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
Product # :
PRO-690Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Lamin A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids and having a molecular mass of 70 kDa. Lamin-A protein is fused to a 6xHis tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Lamin-A Protein solution (0.9mg/ml) contains 20mM phosphate buffer pH 7.0, 500mM NaCl, 1mM DTT, 1.5mM EDTA and 20% (v/v) Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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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, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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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. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRS
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 :
OPG HumanDescription:
Osteoprotegerin Human Recombinant
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-177Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Osteoprotegerin produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of 20kDa. The OPG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OPG was lyophilized from a 0.2µm filtered concentrated (0.5mg/ml) 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 activity is determined by its ability to neutralize the stimulation of U937 cells treated with 10ng/ml of soluble RANKL corresponding to a specific activity of 100,000IU/mg.More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin 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
METFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQK.
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 :
T.pallidum p47Description:
Treponema pallidum p47 Recombinant
Product # :
TRP-243Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the T.Pallidum p47 immunodominant regions. The protein contains beta-galactosidase (114 kDa) fused at the N- terminus.
Source
Escherichia Coli.
Formulation
8M urea, 10mM Tris-HCl pH 8.0, 1mM EDTA and 1mM DTT.
Purity
Treponema Pallidum protein is >95% pure as determined by SDS-PAGE.
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum subsp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Stability
Treponema Pallidum although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.
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Specificity
Immunoreactive with sera of T.Pallidum infected individuals.
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Purification Method
Treponema Pallidum proteinwas purified by proprietary chromatographic technique.
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 :
PTP4A2 HumanDescription:
Protein Tyrosine Phosphatase Type IVA Member 2 Human Recombinant
HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, ptp-IV1a, ptp-IV1b, PTP4A, PTPCAAX2.
Product # :
ENZ-558Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human PTP4A2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-167 a.a.) and having a molecular mass of 23.2 kDa. PTP4A2 is fused to a 36 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The PTP4A2 (0.5mg/ml) protein solution contains 20mM Tris-HCl, pH-8, 1mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PTP4A2 is part of a small class of the protein tyrosine phosphatase (PTP) family. PTP4A2 is localized to the early endosome that take part in a variety of cellular activities. PTP4A2 protein interacts with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), therefore has a role as a regulator of GGT II activity. Overexpression of PTP4A2 in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis.
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Synonyms
HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, ptp-IV1a, ptp-IV1b, PTP4A, PTPCAAX2.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNRP APVEISYENM RFLITHNPTN ATLNKFTEEL KKYGVTTLVR VCDATYDKAP
VEKEGIHVLD WPFDDGAPPP NQIVDDWLNL LKTKFREEPG CCVAVHCVAG LGRAPVLVAL ALIECGMKYE DAVQFIRQKR RGAFNSKQLL
YLEKYRPKMR LRFRDTNGHC CVQ.
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 :
MME Human, ActiveDescription:
Membrane Metalloendopeptidase Human Recombinant, Active
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
Product # :
ENZ-1116Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MME Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 aa) and having a molecular mass of 80.9kDa.MME is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The MME solution (1mg/ml) contains 10% Glycerol, 20 mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 5,000 pmol/min/ug. One unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute, at pH 8.8 at 25C˚.
More Info
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Introduction
Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.
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Synonyms
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
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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
ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISIT NEEDVVVYAP EYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH
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.