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Rabbit anti-Human DYNLL1 Polyclonal Antibody

The antibody against DYNLL1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-89 of human DYNLL1 (NP_003737.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.

ADA-03687A

The antibody against DYNLL1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-89 of human DYNLL1 (NP_003737.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.

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Specifications


Cat.No ADA-03687A ClonalityPolyclonal
Host SpeciesRabbitTarget NameDYNLL1
Target SynonymsLC8; PIN; DLC1; DLC8; LC8a; DNCL1; hdlc1; DNCLC1; DYNLL1FormLiquid
Species ReactivityHuman, MouseIsotypeIgG
Storage Buffer50% Glycerol, PBS with 0.02% sodium azide, pH7.3.Purification MethodAffinity purification
Positive SamplesHeLa, 293T, HepG2, MCF7, Mouse brain, U-251MGApplicationELISA, WB

Immunogen Information


Immunogen DescriptionRecombinant fusion protein containing a sequence corresponding to amino acids 1-89 of human DYNLL1 (NP_003737.1).Target SpeciesHuman
Immunogen SequenceMCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSGUniprot IDP63167
Background Information
  • Uniprot Id

    P63167

  • Target Species

    Human

  • Target Name

    DYNLL1

  • Target Full Name

    Dynein light chain 1, cytoplasmic

  • Target Function

    Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.; Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.; Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.; Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.

  • Target Subcellular Location

    Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Nucleus. Mitochondrion.

  • Target Protein Families

    Dynein light chain family

  • Target Tissue Specificity

    Ubiquitous. Expressed in testis.

  • Target Research Area

    Apoptosis

  • Target Synonyms

    8 kDa dynein light chain; 8kDLC; Cytoplasmic dynein light polypeptide ; DLC1; DLC8; DNCL1; DNCLC1; DYL1_HUMAN; Dynein ; cytoplasmic; light chain 1; Dynein light chain 1 cytoplasmic; Dynein light chain 1; cytoplasmic; Dynein light chain LC8 type 1; Dynein light chain LC8-type 1; Dynein; cytoplasmic; light polypeptide 1; Dynein; light chain; LC8-type 1; DYNLL1; HDLC1; LC8; LC8a; MGC126137; MGC126138; MGC72986; PIN; Protein inhibitor of neuronal nitric oxide synthase; Protein inhibitor of neuronal NOS

  • Target Background

    Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1, 200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.

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